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9xdc

TamAB hybrid barrel state

Method: ELECTRON MICROSCOPY Dmax: 148.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Translocation and assembly module subunit TamA

Escherichia coli str. K-12 substr. MG1655star

UniProt P0ADE4

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 2–577 Not recorded Translocation and assembly module subunit TamB × 1 （P39321） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.69 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 9XDC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
23SP TamA complex with TamB DUF490 in lipid nanodisc Deposited 2026-02-16 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 23–577（555 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.71 Å
23SQ TamA complex with TamB DUF490 in detergent micelles. Deposited 2026-02-16 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 23–577（555 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.51 Å
2LY3 Solution structure of TamA POTRA domain I Deposited 2012-09-11 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain 1 22–102（81 aa） Fragment：C-terminal beta-signal-like motif
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.4；295 K；Ionic strength (raw mmCIF value) 70；Pressure ambient
NMR sample composition 1.8 mM [U-99% 13C; U-99% 15N] TamA domain I, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
4BZA Crystal structure of TamA POTRA domains 1-3 from E. coli Deposited 2013-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–275（254 aa） Fragment：POTRA DOMAINS 1-3, RESIDUES 22-275
Not recorded EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions HEPES PH 7.5, DI-NA TARTRATE, PEG 3350, NACL, GLYCEROL
Resolution 1.84 Å R-free 0.202
4C00 Crystal structure of TamA from E. coli Deposited 2013-07-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–577（556 aa） Fragment：RESIDUES 22-577
Not recorded MC3 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE × 16 ACT ACETATE ION × 2 CL CHLORIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions IMIDAZOLE PH 6.0, NA ACETATE, TRIS, NACL, BETA-OG, DMPC, CHAPSO
Resolution 2.25 Å R-free 0.217
9XDD TamAB in non-hybrid barrel state Deposited 2025-10-27 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–577（576 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.82 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAMA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–577； UniProt 2–577

Translocation and assembly module subunit TamB

Escherichia coli str. K-12 substr. MG1655star

UniProt P39321

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 1–1259 Not recorded Translocation and assembly module subunit TamA × 1 （P0ADE4） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.69 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 9XDC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
23SP TamA complex with TamB DUF490 in lipid nanodisc Deposited 2026-02-16 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 837–1259（423 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.71 Å
23SQ TamA complex with TamB DUF490 in detergent micelles. Deposited 2026-02-16 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 837–1259（423 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.51 Å
5VTG The structure of TamB963-1138 from Escherichia coli reveals a novel hydrophobic Beta-taco fold Deposited 2017-05-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 963–1138（176 aa） Fragment：UNP residues 963-1138
Chain B 963–1138（176 aa） Fragment：UNP residues 963-1138
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；289 K；0.1 M HEPES, 15%(v/v) PEG 400, 0.2 M CaCl2
Resolution 1.86 Å R-free 0.251
9XDD TamAB in non-hybrid barrel state Deposited 2025-10-27 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–1259（1259 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.82 Å

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

View Construct and Data Evidence
UniProt name TAMB_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–1259； UniProt 1–1259

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 9xdc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xdc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xdc
Deposition date deposition_date2025-10-27
Structure title titleTamAB hybrid barrel state
Keywords keywords;outer membrane, interaction, hybrid, TamAB, PROTEIN TRANSPORT, TamA, TamB, lipid transport, outer membrane insertion, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.34 Å
Radius of gyration Rg (electron density) rg_electron41.55 Å
Forward intensity I(0) i0142541000.00
Molecular weight molecular_weight95704.0 kDa
Excluded volume excluded_volume119530 ų
Envelope volume envelope_volume193270 ų
Hydration-shell volume shell_volume41104 ų
Envelope diameter envelope_diameter159.3 Å
Shell Rg shell_rg43.71 Å
Envelope Rg envelope_rg41.56 Å
Shape Rg shape_rg41.56 Å
Total Rg total_rg41.65 Å
Total atoms total_atoms6763
Residues n_residues888
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax148.9 Å
Rg (real space) rg_real41.78 Å
Rg uncertainty (real space) rg_real_error1.69 Å
I(0) (real space) i0_real1.4250e+08
I(0) uncertainty (real space) i0_real_error2.5560e+06
Rg (reciprocal space) rg_reciprocal41.35 Å
I(0) (reciprocal space) i0_reciprocal142500000.0000
Solution quality estimate total_estimate0.8156
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.2 Å
Skewness Skewness skewness0.618
Kurtosis Kurtosis kurtosis-0.025
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12240000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.656
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)