Bam complex
From Proteopedia
(Difference between revisions)
(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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<StructureSection load='4pk1' size='340' side='right' caption='E. coli BamA/BamB (PDB code [[4pk1]])' scene=''> | <StructureSection load='4pk1' size='340' side='right' caption='E. coli BamA/BamB (PDB code [[4pk1]])' scene=''> | ||
| - | The '''Bam''' ( | + | The '''Bam''' (β-Barrel Assembly Machinery) drives the assembly of β-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.<br /> |
| - | *'''BamA''' contains five structurally homologous POTRA (POlypeptide TRAnslocation associated) domains. The POTRA domain has a | + | *'''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.<br /> |
| - | *'''BamD''' is composed of multiple tetratricopeptide (TPR) repeats packed into a superhelical structure. TPR is a motif containing 2 antiparallel | + | *'''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. |
Revision as of 09:37, 12 July 2015
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3D Structures of Bam complex
Updated on 12-July-2015
