Sandbox Reserved 940

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==Introduction==
==Introduction==
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'''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).<ref>PMID:21277859</ref> 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. What is the protein structure? Great Question! Here is a (partial) protein structure: <scene name='57/579693/2jrb_test/1'>Click here</scene>. It you'd like the full-length structure, <scene name='57/579693/2yko_test/1'>click here</scene>. <scene name='57/579693/2yko_test/2'>Check out these metal ions!!!</scene> Name, source, functional description of the family of proteins it represents.
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'''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).<ref>PMID:21277859</ref> 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.
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short description about biology of the system/s where this protein/s takes part.
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==Structure==
==Structure==

Revision as of 14:45, 14 May 2014

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This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947.
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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

STRUCTURE OF A BamB (PDB entry 3Q7M), A PARTIAL STRUCTURE OF LINE-1 ORF1p 2JRB, AND THE FULL-LENGTH STRUCTURE WITH METAL COFACTORS 2YKO

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Additional Information

References

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  1. ↑ 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
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