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| <StructureSection load='4n75' size='340' side='right' caption='E. coli BamA/BamB (PDB code [[4pk1]])' scene=''> | | <StructureSection load='4n75' size='340' side='right' caption='E. coli BamA barrel domain (PDB code [[4n75]])' scene=''> |
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| == Function == | | == Function == |
Revision as of 08:37, 9 November 2015
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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.
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.
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3D Structures of Bam complex
Updated on 09-November-2015
{"openlevels":0}
- 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
