› 2xe1

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb2xe1/pdb
PDB entry 2xe1 coloured by chain, front view.
PDB entry 2xe1 coloured by chain, side view.
PDB entry 2xe1 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
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-184013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane porin C Chain: A
Molecule details ›
Chain: A
Length: 354 amino acids
Theoretical weight: 39.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8CVW1 (Residues: 22-375; Coverage: 100%)
Gene names: c2758, ompC
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

2 bound ligands:
Ligand D10 2 x D10
Ligand HEX 1 x HEX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6322
Unit cell:
a: 120.4Å b: 120.4Å c: 158.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.193 0.218
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

7 mentions without citation

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