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Sandbox Reserved 940

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==Introduction==
==Introduction==
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BamB is the largest of four lipoproteins in the β-barrel assembly machinery (BAM) complex. 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). BamB interacts with the periplasmic domain of BamA, an integral outer membrane protein essential for outer membrane protein biogenesis. The outer membrane contains numerous β-barrel proteins commonly called outer membrane proteins (OMPs), which serve essential functions in cargo transport and signaling and are also vital for membrane biogenesis. OMPs are synthesized in cytoplasm and will be transported to the periplasm by Sec translocon. In the periplasm chaperons (SurA, Skp, and DegP) guide the 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. BamB interact with BamA components (POTRA regions). By doing so BamB act as a scafold 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 is the largest of four lipoproteins in the β-barrel assembly machinery (BAM) complex. 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> ‘<references/>’BamB interacts with the periplasmic domain of BamA, an integral outer membrane protein essential for outer membrane protein biogenesis. The outer membrane contains numerous β-barrel proteins commonly called outer membrane proteins (OMPs), which serve essential functions in cargo transport and signaling and are also vital for membrane biogenesis. OMPs are synthesized in cytoplasm and will be transported to the periplasm by Sec translocon. In the periplasm chaperons (SurA, Skp, and DegP) guide the 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. BamB interact with BamA components (POTRA regions). By doing so BamB act as a scafold 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.
short description about biology of the system/s where this protein/s takes part.
short description about biology of the system/s where this protein/s takes part.

Revision as of 12:49, 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 is the largest of four lipoproteins in the β-barrel assembly machinery (BAM) complex. 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] ‘
  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
’BamB interacts with the periplasmic domain of BamA, an integral outer membrane protein essential for outer membrane protein biogenesis. The outer membrane contains numerous β-barrel proteins commonly called outer membrane proteins (OMPs), which serve essential functions in cargo transport and signaling and are also vital for membrane biogenesis. OMPs are synthesized in cytoplasm and will be transported to the periplasm by Sec translocon. In the periplasm chaperons (SurA, Skp, and DegP) guide the 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. BamB interact with BamA components (POTRA regions). By doing so BamB act as a scafold 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: . It you'd like the full-length structure, . Name, source, functional description of the family of proteins it represents.

short description about biology of the system/s where this protein/s takes part.

Your Heading Here (maybe something like 'Structure')

STRUCTURE OF A THERMOSTABLE LYSOZYME (PDB entry 1L35), 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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