9tg4

Structure of the YbjP lipoprotein bound to the AcrABZ-TolC efflux pump

Method: ELECTRON MICROSCOPY Dmax: 260.8 Å Quality: GOOD

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

Outer membrane protein TolC

Escherichia coli

UniProt P02930

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 × 18 PDB declaration: 18-meric(18) Consistent with protein copy count Chain A; UniProt 23–493 Chain B; UniProt 23–493 Chain C; UniProt 23–493 Not recorded Multidrug efflux pump subunit AcrA × 6 (P0AE06) Multidrug efflux pump subunit AcrB × 3 (P31224) Multidrug efflux pump accessory protein AcrZ × 3 (P0AAW9) Uncharacterized lipoprotein YbjP × 3 (P75818) CL CHLORIDE ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOLC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–472; UniProt 23–493 Author chain B; PDBConstruct 2–472; UniProt 23–493 Author chain C; PDBConstruct 2–472; UniProt 23–493

Multidrug efflux pump subunit AcrA

Escherichia coli

UniProt P0AE06

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 × 18 PDB declaration: 18-meric(18) Consistent with protein copy count Chain D; UniProt 1–397 Chain E; UniProt 1–397 Chain F; UniProt 1–397 Chain G; UniProt 1–397 Chain H; UniProt 1–397 Chain I; UniProt 1–397 Not recorded Outer membrane protein TolC × 3 (P02930) Multidrug efflux pump subunit AcrB × 3 (P31224) Multidrug efflux pump accessory protein AcrZ × 3 (P0AAW9) Uncharacterized lipoprotein YbjP × 3 (P75818) CL CHLORIDE ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACRA_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–397; UniProt 1–397 Author chain E; PDBConstruct 1–397; UniProt 1–397 Author chain F; PDBConstruct 1–397; UniProt 1–397 Author chain G; PDBConstruct 1–397; UniProt 1–397 Author chain H; PDBConstruct 1–397; UniProt 1–397 Author chain I; PDBConstruct 1–397; UniProt 1–397

Multidrug efflux pump subunit AcrB

Escherichia coli

UniProt P31224

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 × 18 PDB declaration: 18-meric(18) Consistent with protein copy count Chain J; UniProt 1–1049 Chain K; UniProt 1–1049 Chain L; UniProt 1–1049 Not recorded Outer membrane protein TolC × 3 (P02930) Multidrug efflux pump subunit AcrA × 6 (P0AE06) Multidrug efflux pump accessory protein AcrZ × 3 (P0AAW9) Uncharacterized lipoprotein YbjP × 3 (P75818) CL CHLORIDE ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

117 other PDB entries and 124 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACRB_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–1049; UniProt 1–1049 Author chain K; PDBConstruct 1–1049; UniProt 1–1049 Author chain L; PDBConstruct 1–1049; UniProt 1–1049

Multidrug efflux pump accessory protein AcrZ

Escherichia coli

UniProt P0AAW9

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 × 18 PDB declaration: 18-meric(18) Consistent with protein copy count Chain M; UniProt 1–49 Chain N; UniProt 1–49 Chain O; UniProt 1–49 Not recorded Outer membrane protein TolC × 3 (P02930) Multidrug efflux pump subunit AcrA × 6 (P0AE06) Multidrug efflux pump subunit AcrB × 3 (P31224) Uncharacterized lipoprotein YbjP × 3 (P75818) CL CHLORIDE ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

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

View Construct and Data Evidence
UniProt name ACRZ_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–49; UniProt 1–49 Author chain N; PDBConstruct 1–49; UniProt 1–49 Author chain O; PDBConstruct 1–49; UniProt 1–49

Uncharacterized lipoprotein YbjP

Escherichia coli

UniProt P75818

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 × 18 PDB declaration: 18-meric(18) Consistent with protein copy count Chain P; UniProt 28–171 Chain Q; UniProt 28–171 Chain R; UniProt 28–171 Not recorded Outer membrane protein TolC × 3 (P02930) Multidrug efflux pump subunit AcrA × 6 (P0AE06) Multidrug efflux pump subunit AcrB × 3 (P31224) Multidrug efflux pump accessory protein AcrZ × 3 (P0AAW9) CL CHLORIDE ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

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

View Construct and Data Evidence
UniProt name YBJP_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 2–145; UniProt 28–171 Author chain Q; PDBConstruct 2–145; UniProt 28–171 Author chain R; PDBConstruct 2–145; UniProt 28–171

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 9tg4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9tg4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9tg4
Deposition date deposition_date2025-11-28
Structure title titleStructure of the YbjP lipoprotein bound to the AcrABZ-TolC efflux pump
Keywords keywords;Multi-drug efflux pump, RND transporter, MacAB-TolC, AcrABZ-TolC, type I secretion, lipoprotein, membrane protein assembly, MEMBRANE PROTEIN, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier92.42
Radius of gyration Rg (electron density) rg_electron94.81
Forward intensity I(0) i07936950000.00
Molecular weight molecular_weight762560.0 kDa
Excluded volume excluded_volume958850 ų
Envelope volume envelope_volume1510800 ų
Hydration-shell volume shell_volume154930 ų
Envelope diameter envelope_diameter346.4
Shell Rg shell_rg65.28
Envelope Rg envelope_rg95.84
Shape Rg shape_rg94.82
Total Rg total_rg94.38
Total atoms total_atoms53653
Residues n_residues7048
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 dmax260.8
Rg (real space) rg_real86.46
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real7.6110e+09
I(0) uncertainty (real space) i0_real_error1.5500e+08
Rg (reciprocal space) rg_reciprocal83.66
I(0) (reciprocal space) i0_reciprocal7729000000.0000
Solution quality estimate total_estimate0.8298
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.4
Skewness Skewness skewness0.564
Kurtosis Kurtosis kurtosis-0.659
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.4936
Highest regularization parameter α highest_alpha1357000000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.615; Stabil: 0.979; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.032

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)