› 2kxx

Solution NMR

NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex

Released:
DOI: 10.2210/pdb2kxx/pdb
PDB entry 2kxx coloured by chain, ensemble of 20 models, front view.
PDB entry 2kxx coloured by chain, ensemble of 20 models, side view.
PDB entry 2kxx coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex.
Kim KH, Kang HS, Okon M, Escobar-Cabrera E, McIntosh LP, Paetzel M
Biochemistry 50 1081-90 (2011)
PMID: 21207987

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein assembly factor BamE Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A937 (Residues: 21-113; Coverage: 99%)
Gene names: JW2598, b2617, bamE, smpA
Sequence domains: SmpA / OmlA family
Structure domains: Beta-lactamase Inhibitory Protein; Chain:B, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The Bam machine: a molecular cooper.
Ricci et al. (2012)
8 more

8 mentions without citation

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