› 2xg6

X-ray diffraction
3.47Å resolution

Molecular insights into clinically isolated OmpC mutants and their role in multi-drug resistance

Released:
DOI: 10.2210/pdb2xg6/pdb
Model geometry
Fit model/data
PDB entry 2xg6 coloured by chain, front view.
PDB entry 2xg6 coloured by chain, side view.
PDB entry 2xg6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli.
Lou H, Chen M, Black SS, Bushell SR, Ceccarelli M, Mach T, Beis K, Low AS, Bamford VA, Booth IR, Bayley H, Naismith JH
OpenAccess logo PLoS One 6 e25825 (2011)
PMID: 22053181

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-191762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porin OmpC Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 343 amino acids
Theoretical weight: 38.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K597 (Residues: 22-364; Coverage: 100%)
Gene names: BKL28_000773, D9D43_01315, DD762_02040, F7N46_15155, F9B07_08225, FKO60_02770, HL563_04725, HLZ39_00670, ompC
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 142.82Å b: 159.725Å c: 164.601Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.261 0.293
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Adaptive and mutational resistance: role of porins and efflux pumps in drug resistance.
Fernández et al. (2012)
13 more

5 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
4 more