Bam complex

Revision as of 12:15, 12 July 2015 by Michal Harel (talk | contribs) (New page: <StructureSection load='4pk1' size='340' side='right' caption='E. coli BamA/BamB (PDB code 4pk1)' scene=''> The '''Bam''' (b-Barrel Assembly Machinery) drives the assembly of b-barrel...)
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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

E. coli BamA/BamB (PDB code 4pk1)

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3D Structures of Bam complex3D Structures of Bam complex

Updated on 12-July-2015

ReferencesReferences

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Michal Harel, Alexander Berchansky, Joel L. Sussman