› 1oyd

X-ray diffraction
3.8Å resolution

Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump

Released:
DOI: 10.2210/pdb1oyd/pdb
PDB 1oyd coloured by chain and viewed from the front.
PDB 1oyd coloured by chain and viewed from the side.
PDB 1oyd coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.
Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE
Science 300 976-80 (2003)
PMID: 12738864

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug efflux pump subunit AcrB Chain: A
Molecule details ›
Chain: A
Length: 1049 amino acids
Theoretical weight: 113.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P31224 (Residues: 1-1049; Coverage: 100%)
Gene names: JW0451, acrB, acrE, b0462
Sequence domains: AcrB/AcrD/AcrF family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DEQ 1 x DEQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: R32
Unit cell:
a: 144.767Å b: 144.767Å c: 517.891Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.287 0.284 0.338
Expression system: Escherichia coli

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Citations

76 review citations

Current Developments in Native Nanometric Discoidal Membrane Bilayer Formed by Amphipathic Polymers.
Esmaili et al. (2021)
75 more

3 mentions without citation

Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.
Kim et al. (2021)
2 more