Bam complex: Difference between revisions

Latest revision as of 13:31, 1 April 2019

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.

3D Structures of Bam complex

Bam complex 3D structures

ReferencesReferences

↑ 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, Alexander Berchansky, Joel L. Sussman

[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

[1]

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