Bam complex: Difference between revisions

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</StructureSection>
</StructureSection>
== 3D Structures of Bam complex ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*BamA (Omp85)
**[[4k3b]] – NgBamA – ''Neisseria gonorrhoeae'' <br />
**[[4k3c]] – BamA – ''Haemophilus ducreyi'' <br />
**[[5or1]] – BamA – Salmonella typhimurium<br />
**[[2qcz]], [[2qdf]] – EcBamA residues 21-351 – ''Escherichia coli'' <br />
**[[3q6b]] – EcBamA POTRA1-2 domain residues 21-174<br />
**[[3efc]] – EcBamA periplasmic domain residues 21-410<br />
**[[4c4v]] – EcBamA residues 344-808 <br />
**[[4pk1]] – EcBamA/BamB <br />
**[[4n75]], [[6fsu]] – EcBamA barrel domain residues 427-810<br />
**[[3og5]], [[3q6b]] – EcBamA POTRA45 domain residues 264-424<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]] – RmBamD residues 24-280 – ''Rhodothermus marinus''<br />
**[[3tgo]] – EcBamD residues 21-245 + lipoprotein 34<br />
**[[5waq]] – NgBamD<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 />
**[[5wam]] – NgBamE<br />
*BamA+BamB
**[[4xga]] – EcBam  <br />
*BamA+BamD
**[[5efr]] – RmBam  <br />
*BamA+BamC+BamD+BamE
**[[5ekq]], [[5d0q]] – EcBam  <br />
*BamA+BamB+BamC+BamD+BamE
**[[5d0o]], [[5ayw]] – EcBam  <br />
**[[5ljo]] – EcBam – Cryo EM <br />
}}


== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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, Alexander Berchansky, Joel L. Sussman
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