Sandbox Reserved 940
From Proteopedia
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===Active site organisation=== | ===Active site organisation=== | ||
| - | The active site of BamB are found in | + | The active site of BamB are found in <scene name='57/579710/3q7m_-_interactive_site/2'>BamB interactive sites </scene>. |
Revision as of 16:59, 15 May 2014
Contents |
Introduction
BamB (PDB entry:3Q7M)is one of the lipoprotein found in the β-barrel assembly machinery (BAM) complex in outer membrane of Escherichia coli. The E. coli BAM complex consists of five subunits named BamA (88 kDa), BamB (40 kDa), BamC (34 kDa), BamD (26 kDa) and BamE (10 kDa).[1] The outer membrane contains numerous β-barrel proteins commonly called outer membrane proteins (OMPs), which serve as in cargo transport and signaling and are also vital for membrane biogenesis. OMPs are synthesized in cytoplasm and transported to the periplasm by Sec translocon. With in the periplasm, chaperones (SurA, Skp, and DegP) guide the OMPs to the BAM complex. BAM complex function by folding and inserting the new OMPs into the outer membrane. Here BamB, while non-essential, plays an important role in the assembly of OMPs by interacting with the BamA components(POTRA regions). Thus BamB act as a scaffold to optimally orient POTRA regions for interaction with other BAM components, chaperones, and nascent OMPs.
Structure
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Additional Information
References
‘- ↑ Noinaj N, Fairman JW, Buchanan SK. The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex. J Mol Biol. 2011 Jan 26. PMID:21277859 doi:10.1016/j.jmb.2011.01.042
