› 3prw

X-ray diffraction
1.8Å resolution

Crystal structure of the lipoprotein BamB

Released:
DOI: 10.2210/pdb3prw/pdb
PDB entry 3prw coloured by chain, front view.
PDB entry 3prw coloured by chain, side view.
PDB entry 3prw coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Augmenting β-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins.
Heuck A, Schleiffer A, Clausen T
J Mol Biol 406 659-66 (2011)
PMID: 21236263

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-160199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein assembly factor BamB Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 40.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77774 (Residues: 21-392; Coverage: 100%)
Gene names: JW2496, b2512, bamB, yfgL
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 50.221Å b: 120.967Å c: 134.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

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

6 mentions without citation

The bacterial outer membrane β-barrel assembly machinery.
Kim et al. (2012)
5 more