8tvr

In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution

Method: ELECTRON MICROSCOPY D_max: 194.2 Å Quality: GOOD

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Tail spike protein

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–667 Chain B； UniProt 1–667 Chain C； UniProt 1–667 Chain D； UniProt 1–667 Chain E； UniProt 1–667 Chain F； UniProt 1–667 Chain H； UniProt 1–667 Chain I； UniProt 1–667 Chain J； UniProt 1–667 Chain L； UniProt 1–667 Chain M； UniProt 1–667 Chain N； UniProt 1–667 Chain P； UniProt 1–667 Chain Q； UniProt 1–667 Chain R； UniProt 1–667 Chain V； UniProt 1–667 Chain W； UniProt 1–667 Chain X； UniProt 1–667	Not recorded	Packaged DNA stabilization protein gp10 × 6 （P26749）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 8TVR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CLW TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT Deposited 1999-05-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 114–667（554 aa） Fragment：CATALYTIC FRAGMENT	Mutation：V331A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；pH 10.00	Resolution 2.00 Å
1CLW TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT Deposited 1999-05-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：CATALYTIC FRAGMENT	Mutation：V331A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；pH 10.00	Resolution 2.00 Å
1LKT CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN Deposited 1997-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN Chain B 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN Chain C 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.6；20% PEG 8K, 0.2 M MGCL2, 0.1 M BIS-TRIS, PH 6.6	Resolution 2.60 Å
1LKT CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN Deposited 1997-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN Chain E 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN Chain F 6–109（104 aa） Fragment：HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.6；20% PEG 8K, 0.2 M MGCL2, 0.1 M BIS-TRIS, PH 6.6	Resolution 2.60 Å
1QA1 TAILSPIKE PROTEIN, MUTANT V331G Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL DOMAIN	Mutation：V331G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；274 K；VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QA1 TAILSPIKE PROTEIN, MUTANT V331G Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL DOMAIN	Mutation：V331G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；274 K；VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QA2 TAILSPIKE PROTEIN, MUTANT A334V Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT	Mutation：A334V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QA2 TAILSPIKE PROTEIN, MUTANT A334V Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT	Mutation：A334V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QA3 TAILSPIKE PROTEIN, MUTANT A334I Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT	Mutation：A334I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QA3 TAILSPIKE PROTEIN, MUTANT A334I Deposited 1999-04-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RECEPTOR BINDING C-TERMINAL FRAGMENT	Mutation：A334I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277 K；VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE	Resolution 2.00 Å
1QQ1 TAILSPIKE PROTEIN, MUTANT E359G Deposited 1999-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT	Mutation：E359G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE, 0.1M SODIUM PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å
1QRB PLASTICITY AND STERIC STRAIN IN A PARALLEL BETA-HELIX: RATIONAL MUTATIONS IN P22 TAILSPIKE PROTEIN Deposited 1999-06-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT	Mutation：T326F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE 0.1 M SODIUM PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å
1QRC TAILSPIKE PROTEIN, MUTANT W391A Deposited 1999-06-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 109–667（559 aa） Fragment：C-TERMINAL FRAGMENT	Mutation：W391A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；1M AMMONIUM SULPHATE, 0.1M NA-PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å
1TSP CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER Deposited 1994-06-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 109–667（559 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1TYU STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA ENTERITIDIS AT PH 7.5	Resolution 1.80 Å
1TYV STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 1.80 Å
1TYW STRUCTURE OF TAILSPIKE-PROTEIN Deposited 1996-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH DECASACCHARIDE FROM S. TYPHI 253TY O-ANTIGEN AT PH 7.5	Resolution 1.80 Å
1TYX TITLE OF TAILSPIKE-PROTEIN Deposited 1996-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 114–667（554 aa） Fragment：RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA TYPHIMURIUM O-ANTIGEN AT PH 7.5.	Resolution 1.80 Å
2VFM Low Temperature Structure of P22 Tailspike Protein Fragment (109-666) Deposited 2007-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 110–667（558 aa） Fragment：RESIDUES 110-667	Not recorded	GOL GLYCEROL × 33 SO4 SULFATE ION × 6 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0	Resolution 1.50 Å R-free 0.164
2VFN Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A Deposited 2007-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 110–667（558 aa） Fragment：RESIDUES 110-667	Mutation：YES	GOL GLYCEROL × 30 SO4 SULFATE ION × 3 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER, 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0	Resolution 1.50 Å R-free 0.155
2VFO Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L Deposited 2007-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 110–667（558 aa） Fragment：RESIDUES 110-667	Mutation：YES	GOL GLYCEROL × 21 SO4 SULFATE ION × 3 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0	Resolution 1.50 Å R-free 0.144
2VFP Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L Deposited 2007-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 110–667（558 aa） Fragment：RESIDUES 110-667	Mutation：YES	GOL GLYCEROL × 18 SO4 SULFATE ION × 3 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0	Resolution 1.55 Å R-free 0.152
2VFQ Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V450A Deposited 2007-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 110–667（558 aa） Fragment：RESIDUES 110-667 LACKING THE N-TERMINAL HEAD-BINDING DOMAIN	Mutation：YES	GOL GLYCEROL × 12 SO4 SULFATE ION × 6 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0	Resolution 1.55 Å R-free 0.145
2VKY Headbinding Domain of Phage P22 Tailspike C-Terminally Fused to Isoleucine Zipper pIIGCN4 (Chimera I) Deposited 2008-01-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 2–124（123 aa） Fragment：HEAD-BINDING DOMAIN, RESIDUES 2-124	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；VAPOR DIFFUSION, HANGING DROP. PROTEIN: CONC. 8.2 MG/ML,BUFFER 50MM HEPES, PH6.5; RESERVOIR: 20% ISOPROPANOL, 0.1M NA-ACETATE, PH4.6, 0.2M CACL2; DROPLET 2 MICROL: 2 MICROL.CRYO:30% GLYCEROL.	Resolution 2.05 Å R-free 0.187
2VNL MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II) Deposited 2008-02-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 2–122（121 aa） Fragment：HEAD-BINDING DOMAIN, RESIDUES 2-122	Mutation：YES	GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；VAPOR DIFFUSION, HANGING DROP. PROTEIN: CONC. 9.3 MG/ML,BUFFER 50MM HEPES, PH6.5; RESERVOIR:20% ISOPROPANOL, 0.1M NA-ACETATE, PH4.6, 0.2M CACL2; DROPLET 2 MICROL:2 MICROL.CRYO:30% GLYCEROL.	Resolution 1.80 Å R-free 0.229
2XC1 Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22 Deposited 2010-04-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 2–667（666 aa） Fragment：RESIDUES 2-667 Chain B 2–667（666 aa） Fragment：RESIDUES 2-667 Chain C 2–667（666 aa） Fragment：RESIDUES 2-667	Mutation：YES Mutation：YES Mutation：YES	GOL GLYCEROL × 13 CA CALCIUM ION × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 4 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；PROTEIN- 15MG/ML IN 10MM HEPES PH7;RESERVOIR:750 ML 0.2M AMMONIUM ACETATE,0.1M TRI-SODIUM CITRATE DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE GLYCOL 4000; HANGING DROPS:1.5MICROL RESERVOIR- 1.5MICROL PROTEIN SOLUTION; TEMPERATURE: 19 DEGR.; CRYO: 3% GLYCEROL	Resolution 1.65 Å R-free 0.210
3TH0 P22 Tailspike complexed with S.Paratyphi O antigen octasaccharide Deposited 2011-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 109–667（559 aa） Fragment：UNP residues 109-657	Not recorded	GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；277.15 K；1.5 Ammonium sulfate, 0.1M sodium phosphate over reservoir 1.0 Ammonium sulfate, 0.1M sodium phosphate, pH 10, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K X-ray crystallization conditions MICRODIALYSIS；pH 7.5；293.15 K；addition of 2mM S.Paratyphi o antigen octasaccharide in 0.1M Tris, 1M sodium phosphate, pH 7.5, MICRODIALYSIS, temperature 293.15K	Resolution 1.75 Å R-free 0.156
5GAI Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins Deposited 2015-12-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric	Chain 0 6–667（662 aa） Chain Y 6–667（662 aa） Chain Z 6–667（662 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2 seconds before plunging.	Resolution 10.50 Å
8EAN Cryo-EM structure of in-situ tailspike in bacteriophage P22 Deposited 2022-08-29	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 0 6–667（662 aa） Chain Y 6–667（662 aa） Chain Z 6–667（662 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8EB7 Cryo-EM structure of the in-situ gp4-gp10-gp9N from bacteriophage P22 Deposited 2022-08-30	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 0 6–116（111 aa） Chain A 6–116（111 aa） Chain B 6–116（111 aa） Chain C 6–116（111 aa） Chain D 6–116（111 aa） Chain F 6–116（111 aa） Chain X 6–116（111 aa） Chain Y 6–116（111 aa） Chain Z 6–116（111 aa） Chain a 6–116（111 aa） Chain b 6–116（111 aa） Chain c 6–116（111 aa） Chain d 6–116（111 aa） Chain e 6–116（111 aa） Chain f 6–116（111 aa） Chain g 6–116（111 aa） Chain h 6–116（111 aa） Chain i 6–116（111 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain 10 1–667（667 aa） Chain 11 1–667（667 aa） Chain 12 1–667（667 aa） Chain 13 1–667（667 aa） Chain 14 1–667（667 aa） Chain 15 1–667（667 aa） Chain 16 1–667（667 aa） Chain 17 1–667（667 aa） Chain 18 1–667（667 aa） Chain 19 1–667（667 aa） Chain 20 1–667（667 aa） Chain 21 1–667（667 aa） Chain 22 1–667（667 aa） Chain 23 1–667（667 aa） Chain 24 1–667（667 aa） Chain 7 1–667（667 aa） Chain 8 1–667（667 aa） Chain 9 1–667（667 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain 10 1–667（667 aa） Chain 11 1–667（667 aa） Chain 12 1–667（667 aa） Chain 13 1–667（667 aa） Chain 14 1–667（667 aa） Chain 15 1–667（667 aa） Chain 16 1–667（667 aa） Chain 17 1–667（667 aa） Chain 18 1–667（667 aa） Chain 19 1–667（667 aa） Chain 20 1–667（667 aa） Chain 21 1–667（667 aa） Chain 22 1–667（667 aa） Chain 23 1–667（667 aa） Chain 24 1–667（667 aa） Chain 7 1–667（667 aa） Chain 8 1–667（667 aa） Chain 9 1–667（667 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8U1O In situ cryo-EM structure of bacteriophage P22 tailspike protein complex at 3.4A resolution Deposited 2023-09-01	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain o 1–667（667 aa） Chain p 1–667（667 aa） Chain q 1–667（667 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FIBER_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–667； UniProt 1–667 Author chain B； PDBConstruct 1–667； UniProt 1–667 Author chain C； PDBConstruct 1–667； UniProt 1–667 Author chain D； PDBConstruct 1–667； UniProt 1–667 Author chain E； PDBConstruct 1–667； UniProt 1–667 Author chain F； PDBConstruct 1–667； UniProt 1–667 Author chain H； PDBConstruct 1–667； UniProt 1–667 Author chain I； PDBConstruct 1–667； UniProt 1–667 Author chain J； PDBConstruct 1–667； UniProt 1–667 Author chain L； PDBConstruct 1–667； UniProt 1–667 Author chain M； PDBConstruct 1–667； UniProt 1–667 Author chain N； PDBConstruct 1–667； UniProt 1–667 Author chain P； PDBConstruct 1–667； UniProt 1–667 Author chain Q； PDBConstruct 1–667； UniProt 1–667 Author chain R； PDBConstruct 1–667； UniProt 1–667 Author chain V； PDBConstruct 1–667； UniProt 1–667 Author chain W； PDBConstruct 1–667； UniProt 1–667 Author chain X； PDBConstruct 1–667； UniProt 1–667

Packaged DNA stabilization protein gp10

OrganismNot specified

UniProt P26749

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain G； UniProt 1–472 Chain K； UniProt 1–472 Chain O； UniProt 1–472 Chain S； UniProt 1–472 Chain T； UniProt 1–472 Chain Y； UniProt 1–472	Not recorded	Tail spike protein × 18 （P12528）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8TVR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8EAP Cryo-EM structure of the in-situ gp10-gp26 from bacteriophage P22 Deposited 2022-08-29	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain D 2–472（471 aa） Chain E 2–472（471 aa） Chain F 2–472（471 aa） Chain G 2–472（471 aa） Chain H 2–472（471 aa） Chain I 2–472（471 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8EB7 Cryo-EM structure of the in-situ gp4-gp10-gp9N from bacteriophage P22 Deposited 2022-08-30	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain R 2–472（471 aa） Chain S 2–472（471 aa） Chain T 2–472（471 aa） Chain U 2–472（471 aa） Chain V 2–472（471 aa） Chain W 2–472（471 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain 1 1–472（472 aa） Chain 2 1–472（472 aa） Chain 3 1–472（472 aa） Chain 4 1–472（472 aa） Chain 5 1–472（472 aa） Chain 6 1–472（472 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain 1 1–472（472 aa） Chain 2 1–472（472 aa） Chain 3 1–472（472 aa） Chain 4 1–472（472 aa） Chain 5 1–472（472 aa） Chain 6 1–472（472 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VG10_BPP22
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–472； UniProt 1–472 Author chain K； PDBConstruct 1–472； UniProt 1–472 Author chain O； PDBConstruct 1–472； UniProt 1–472 Author chain S； PDBConstruct 1–472； UniProt 1–472 Author chain T； PDBConstruct 1–472； UniProt 1–472 Author chain Y； PDBConstruct 1–472； UniProt 1–472

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	8tvr
Deposition date deposition_date	2023-08-18
Structure title title	In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution
Keywords keywords	;phage, bacteriophage, tail spike protein, TSP, gene product 9 (gp9), Packaged DNA stabilization protein, gene product 10 (gp10), STRUCTURAL PROTEIN, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	59.76 Å
Radius of gyration Rg (electron density) rg_electron	59.34 Å
Forward intensity I(0) i0	4187840000.00
Molecular weight molecular_weight	546340.0 kDa
Excluded volume excluded_volume	683450 Å³
Envelope volume envelope_volume	969280 Å³
Hydration-shell volume shell_volume	132920 Å³
Envelope diameter envelope_diameter	201.0 Å
Shell Rg shell_rg	65.14 Å
Envelope Rg envelope_rg	57.83 Å
Shape Rg shape_rg	59.38 Å
Total Rg total_rg	59.32 Å
Total atoms total_atoms	38532
Residues n_residues	4950
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	194.2 Å
Rg (real space) rg_real	59.49 Å
Rg uncertainty (real space) rg_real_error	2.13 Å
I(0) (real space) i0_real	4.1880e+09
I(0) uncertainty (real space) i0_real_error	9.5300e+07
Rg (reciprocal space) rg_reciprocal	59.96 Å
I(0) (reciprocal space) i0_reciprocal	4191000000.0000
Solution quality estimate total_estimate	0.8740
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	74.7 Å
Skewness Skewness skewness	0.170
Kurtosis Kurtosis kurtosis	-0.439
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	150600000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.811

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Tail spike protein
Molecular weight formula_weight	71923.5 kDa
Source method src_method	nat
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,H,I,J,L,M,N,P,Q,R,V,W,X
Atom count atom_count	38532

MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGESGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDMNPELDRPGDYPITQYPLHQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIIDTNTKDFQANQIYISGACRVNGLRLIGIRSTDGQGLTIDAPNSTVSGITGMVDPSRINVANLAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGSTPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELVRLTLATL

Entity 2 Entity 2 polymer

Description description	Packaged DNA stabilization protein gp10
Molecular weight formula_weight	52512.0 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S,G,K,O,T,Y

MPIQQLPMMKGMGKDFKNADYIDYLPVNMLATPKEILNSSGYLRSFPGITKRYDMNGVSRGVEYNTAQNAVYRVCGGKLYKGESEVGDVAGSGRVSMAHGRTSQAVGVNGQLVEYRYDGTVKTVSNWPADSGFTQYELGSVRDITRLRGRYAWSKDGTDSWFITDLEDESHPDRYSAQYRAESQPDGIIGIGTWRDFIVCFGSSTIEYFSLTGATTAGAALYVAQPSLMVQKGIAGTYCKTPFADSYAFISHPATGAPSVYIIGSGQASPIATASIEKIIRSYTAEEMATGVMETLRFDSHELLIIHLPRHVLVYDASSSQNGPQWCVLKTGLYDDVYRGVDFMYEGNQITCGDKSEAVVGQLQFDISSQYDKQQEHLLFTPLFKADNARCFDLEVESSTGVAQYADRLFLSATTDGINYGREQMIEQNEPFVYDKRVLWKRVGRIRRLIGFKLRVITKSPVTLSGCQIRLE

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	38155

fit	/app/data/saxs_computation/tv/8tvr/8tvr.fit
pddf	/app/data/pr_computation/tv/8tvr/8tvr.pr.out
profile	/app/data/saxs_computation/tv/8tvr/8tvr.dat

In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution

1. Protein Identity and Related Structures Protein Identity & Related Structures

Tail spike protein

State in the Current Structure

Other States of the Same Protein in the Database

Packaged DNA stabilization protein gp10

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)