Crystal structure of BamB from Pseudomonas aeruginosa and functional evaluation of its conserved structural features.

ABSTRACT: The assembly of β-barrel Outer Membrane Proteins (OMPs) in the outer membrane is essential for gram-negative bacteria. The process requires the β-Barrel Assembly Machine (BAM), a multiprotein complex that, in E. coli, is composed of the OMP BamA and four lipoproteins BamB-E. Whereas BamA and BamD are essential, deletion of BamB, C or E produce membrane permeability defects. Here we present the high-resolution structure of BamB from Pseudomonas aeruginosa. This protein can complement the deletion of bamB in E. coli indicating that they are functionally equivalent. Conserved structural features include an eight-bladed β-propeller fold stabilized by tryptophan docking motifs with a central pore about 8 Å in diameter at the narrowest point. This pore distinguishes BamB from related β-propeller

SUBMITTER: Jansen KB 

PROVIDER: S-EPMC3506653 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature