The Bam (b-Barrel Assembly Machinery) drives the assembly of b-barrel proteins into the outer membrane of gram-negative bacteria. The complex is composed of five subunits: BamA, BamB, BamC, BamD and BamE. Outer membrane b-barrel proteins assembly is dependent on Bam in various organisms. BamB,C,D,E bind to the N-terminal of BamA.
- BamA contains five structurally homologous POTRA (POlypeptide TRAnslocation associated) domains. The POTRA domain has a b-a-a-b-b conformation. BamA barrel and at least a subset of its POTRAs are essential for viability. BamA was found also in mitochondria and chloroplasts.
- BamD is composed of multiple tetratricopeptide (TPR) repeats packed into a superhelical structure. TPR is a motif containing 2 antiparallel a-helices. TPRs are found in scaffold multiprotein complexes and are involved in protein-protein interactions.
Function
Disease
Relevance
Structural highlights
