Sandbox Reserved 940
From Proteopedia
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===Interactions with other molecules=== | ===Interactions with other molecules=== | ||
| - | BamB interact with BamA through residues[[http://www.proteopedia.org/wiki/images/1/18/BamB_active_site.png]] (L192, L194, R195, D246, and D248). These residues are found on IL4 [[http://www.proteopedia.org/wiki/images/ | + | BamB interact with BamA through residues[[http://www.proteopedia.org/wiki/images/1/18/BamB_active_site.png]] (L192, L194, R195, D246, and D248). These residues are found on IL4 [[http://www.proteopedia.org/wiki/images/5/5f/BamB_active_sites.png]]( L192, L194, R195) and IL5 (D246, D248). BamB interacts with the PORTA 2-4 regions of BamA. The IL4 of the BamB (R195)protein interact with the PORTA 3 regions of the BamA(D241)region by forming a salt bridge. BamB coordinates or optimally arranged the PORTA domains for nascent OMP recognition and insertion.BamB form a triple complex: BamB-BamA-SurA and mediate the interaction between BamA and SurA. This facilitates the delivery, folding and insertion of OMPs into the outer membrane. interact with the Close up picture, with explanation what we see |
===Active site organisation=== | ===Active site organisation=== | ||
Revision as of 18:52, 18 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 polypeptide transport-associated(POTRA regions). Thus BamB act as a scaffold to optimally orient POTRA regions for interaction with other BAM components, chaperones, and nascent OMPs. BamB is not essential for the bacteria because it can survive without it but it is noticed also now that BamB is essential for folding efficiency of 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
![[1]](http://www.proteopedia.org/wiki/images/1/18/BamB_active_site.png){kind=link}
![[2]](http://www.proteopedia.org/wiki/images/5/5f/BamB_active_sites.png){kind=link}