Bam complex: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
<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''' (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 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.


== Function ==
== Function ==


== Disease ==
The '''Bam''' (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria. 


== Relevance ==
== Structural highlights ==


== 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.<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.


</StructureSection>
</StructureSection>

Revision as of 11:34, 9 November 2015


Function

The Bam (β-Barrel Assembly Machinery) drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria.

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.


E. coli BamA/BamB (PDB code 4pk1)

Drag the structure with the mouse to rotate

3D Structures of Bam complex3D Structures of Bam complex

Updated on 09-November-2015

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman