› 2k0l

Solution NMR

NMR structure of the transmembrane domain of the Outer Membrane Protein A from Klebsiella pneumoniae in DHPC micelles.

Released:
DOI: 10.2210/pdb2k0l/pdb
PDB entry 2k0l coloured by chain, ensemble of 20 models, front view.
PDB entry 2k0l coloured by chain, ensemble of 20 models, side view.
PDB entry 2k0l coloured by chain, ensemble of 20 models, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications.
Renault M, Saurel O, Czaplicki J, Demange P, Gervais V, Löhr F, Réat V, Piotto M, Milon A
J Mol Biol 385 117-30 (2009)
PMID: 18952100

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150144 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein A Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.39 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P24017 (Residues: 1-207; Coverage: 60%)
Gene name: ompA
Sequence domains: OmpA-like transmembrane domain
Structure domains: Porin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DGSA-distance geometry simulated annealing, simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins.
Hiller et al. (2009)
4 more

9 mentions without citation

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