› 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
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-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