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| <StructureSection load='4pk1' size='340' side='right' caption='E. coli BamA/BamB (PDB code [[4pk1]])' scene=''> | | <StructureSection load='' size='340' side='right' caption='E. coli BamA barrel domain (PDB code [[4n75]])' scene='70/706705/Cv/2'> |
| 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 ==
| | 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> | | 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. |
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| == 3D Structures of Bam complex == | | == 3D Structures of Bam complex == |
| | [[Bam complex 3D structures]] |
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| | </StructureSection> |
| {{#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/> |
| | [[Category:Topic Page]] |
