› 2gif

X-ray diffraction
2.9Å resolution

Asymmetric structure of trimeric AcrB from Escherichia coli

Released:
DOI: 10.2210/pdb2gif/pdb
PDB entry 2gif coloured by chain, front view.
PDB entry 2gif coloured by chain, side view.
PDB entry 2gif coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism.
Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM
Science 313 1295-8 (2006)
PMID: 16946072

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug efflux pump subunit AcrB Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 1057 amino acids
Theoretical weight: 114.74 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 FLC 2 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 222.8Å b: 134.1Å c: 161.01Å
α: 90° β: 98.21° γ: 90°
R-values:
R R work R free
0.228 0.226 0.267
Expression system: Escherichia coli

Quick links

Citations

81 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
80 more

29 mentions without citation

Assembly and transport mechanism of tripartite drug efflux systems.
Misra et al. (2009)
28 more