Bam complex

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<StructureSection load='4pk1' size='340' side='right' caption='E. coli BamA/BamB (PDB code [[4pk1]])' scene=''>
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<StructureSection load='' size='340' side='right' caption='E. coli BamA barrel domain (PDB code [[4n75]])' scene='70/706705/Cv/2'>
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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 />
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*'''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 />
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*'''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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== Function ==
== Function ==
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== Disease ==
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The '''Bam''' (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria.<ref>PMID:19182809</ref>
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== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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</StructureSection>
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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.<br />
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*'''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 />
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*'''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.
== 3D Structures of Bam complex ==
== 3D Structures of Bam complex ==
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[[Bam complex 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*BamA (Omp85)
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**[[4k3b]] – BamA – ''Neisseria gonorrhoeae'' <br />
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**[[4k3c]] – BamA – ''Haemophilus ducreyi'' <br />
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**[[4c4v]] – EcBamA – ''Escherichia coli'' <br />
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**[[4pk1]] – EcBamA/BamB <br />
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**[[4n75]] – EcBamA barrel domain<br />
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**[[3og5]], [[3q6b]] – EcBamA POTRA45 domain<br />
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*BamB (Lipoprotein YFGL)
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**[[3q7m]], [[3q7n]], [[3q7o]], [[3p1l]], [[2yms]] – EcBamB <br />
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**[[3q54]], [[3prw]], [[2yh3]] – EcBamB residues 25-392 <br />
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**[[4hdj]] – BamB residues 20-380 – ''Pseudomonas aeruginosa''<br />
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**[[4imm]] – BamB – ''Moraxella catarrhalis'' <br />
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*BamC (Lipoprotein 34)
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**[[2yh5]], [[3sns]] – EcBamC C terminal <br />
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**[[2lae]] – EcBamC C terminal - NMR <br />
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**[[2yh6]] – EcBamC N terminal <br />
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**[[2laf]] – EcBamC N terminal - NMR <br />
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*BamD (Lipoprotein YFIO)
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**[[2yhc]], [[3q5m]] – EcBamD residues 29-245 <br />
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**[[3qky]] – BamD residues 24-280 – ''Rhodothermus marinus''<br />
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**[[3tgo]] – EcBamD residues 21-245 + lipoprotein 34<br />
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*BamE (Small protein A)
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**[[2yh9]] – EcBamE residues 34-113 <br />
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**[[2kxx]] – EcBamE residues 21-114 - NMR <br />
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**[[2km7]] – EcBamE residues 21-114 (mutant) - NMR <br />
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}}
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== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

E. coli BamA barrel domain (PDB code 4n75)

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References

  1. ↑ 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:http://dx.doi.org/10.1038/nrmicro2069

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Michal Harel, Joel L. Sussman, Alexander Berchansky

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