6p22

Photorhabdus Virulence Cassette (PVC) PAAR repeat protein Pvc10 in complex with a T4 gp5 beta-helix fragment modified to mimic Pvc8, the central spike protein of PVC

Method: X-RAY DIFFRACTION Dmax: 115.0 Å Quality: REASONABLE

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

CHIMERA OF CENTRAL SPIKE PROTEINS GP5 FROM PHAGE T4 AND PVC8 FROM PVC

Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)

UniProt P16009

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 484–565 Chain B; UniProt 484–565 Chain C; UniProt 484–565 Not recorded PAAR-REPEAT CENTRAL SPIKE TIP PROTEIN × 1 (Q7N648) MG MAGNESIUM ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;MPD 28-34% PEG 2000 8-18% 100 mM Imidazole pH 8.0 Resolution 2.29 Å R-free 0.222

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.

17 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BP5_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–86; UniProt 484–565 Author chain B; PDBConstruct 5–86; UniProt 484–565 Author chain C; PDBConstruct 5–86; UniProt 484–565

CHIMERA OF CENTRAL SPIKE PROTEINS GP5 FROM PHAGE T4 AND PVC8 FROM PVC

Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)

UniProt Q7N647

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 523–533 Chain B; UniProt 523–533 Chain C; UniProt 523–533 Not recorded PAAR-REPEAT CENTRAL SPIKE TIP PROTEIN × 1 (Q7N648) MG MAGNESIUM ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;MPD 28-34% PEG 2000 8-18% 100 mM Imidazole pH 8.0 Resolution 2.29 Å R-free 0.222

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7N647_PHOLL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 87–97; UniProt 523–533 Author chain B; PDBConstruct 87–97; UniProt 523–533 Author chain C; PDBConstruct 87–97; UniProt 523–533

PAAR-REPEAT CENTRAL SPIKE TIP PROTEIN

Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)

UniProt Q7N648

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–138 Not recorded CHIMERA OF CENTRAL SPIKE PROTEINS GP5 FROM PHAGE T4 AND PVC8 FROM PVC × 3 (P16009,Q7N647) MG MAGNESIUM ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;MPD 28-34% PEG 2000 8-18% 100 mM Imidazole pH 8.0 Resolution 2.29 Å R-free 0.222

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q7N648_PHOLL
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–138; UniProt 1–138

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

SAXS profile for 6p22

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6p22
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6p22
Deposition date deposition_date2019-05-20
Structure title titlePhotorhabdus Virulence Cassette (PVC) PAAR repeat protein Pvc10 in complex with a T4 gp5 beta-helix fragment modified to mimic Pvc8, the central spike protein of PVC
Keywords keywords;PVC, Photorhabdus laumondii, membrane piercing, central spike, cell puncturing device, PAAR-repeat motif, beta helix, T4 gp5, contractile injection system, viral protein, Pvc8, Pvc10, hydrolase ;; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.93
Radius of gyration Rg (electron density) rg_electron30.78
Forward intensity I(0) i033308800.00
Molecular weight molecular_weight44774.0 kDa
Excluded volume excluded_volume56007 ų
Envelope volume envelope_volume67573 ų
Hydration-shell volume shell_volume21925 ų
Envelope diameter envelope_diameter118.8
Shell Rg shell_rg31.80
Envelope Rg envelope_rg31.79
Shape Rg shape_rg30.77
Total Rg total_rg30.90
Total atoms total_atoms6301
Residues n_residues419
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax115.0
Rg (real space) rg_real30.70
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real3.3310e+07
I(0) uncertainty (real space) i0_real_error5.0330e+05
Rg (reciprocal space) rg_reciprocal30.37
I(0) (reciprocal space) i0_reciprocal33300000.0000
Solution quality estimate total_estimate0.6600
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.855
Kurtosis Kurtosis kurtosis0.205
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6283000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.200; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.098; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (3)

9. Files and Curves (10)