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Function
The Bam (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria.[1]
Structural highlights
The complex is composed of five subunits: BamA, BamB, BamC, BamD and BamE. Outer membrane β-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 β-α-α-β-β 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 α-helices. TPRs are found in scaffold multiprotein complexes and are involved in protein-protein interactions.
- ↑ Knowles TJ, Scott-Tucker A, Overduin M, Henderson IR. Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol. 2009 Mar;7(3):206-14. doi: 10.1038/nrmicro2069. Epub 2009 Feb , 2. PMID:19182809 doi:https://dx.doi.org/10.1038/nrmicro2069
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3D Structures of Bam complex
Updated on 13-January-2016
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- BamA (Omp85)
- 4k3b – BamA – Neisseria gonorrhoeae
- 4k3c – BamA – Haemophilus ducreyi
- 4c4v – EcBamA – Escherichia coli
- 4pk1 – EcBamA/BamB
- 4n75 – EcBamA barrel domain
- 3og5, 3q6b – EcBamA POTRA45 domain
- BamB (Lipoprotein YFGL)
- BamC (Lipoprotein 34)
- 2yh5, 3sns – EcBamC C terminal
- 2lae – EcBamC C terminal - NMR
- 2yh6 – EcBamC N terminal
- 2laf – EcBamC N terminal - NMR
- BamD (Lipoprotein YFIO)
- 2yhc, 3q5m – EcBamD residues 29-245
- 3qky – BamD residues 24-280 – Rhodothermus marinus
- 3tgo – EcBamD residues 21-245 + lipoprotein 34
- BamE (Small protein A)
- 2yh9 – EcBamE residues 34-113
- 2kxx – EcBamE residues 21-114 - NMR
- 2km7 – EcBamE residues 21-114 (mutant) - NMR
References
