We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Sandbox Reserved 940

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
+
<Structure load='3Q7M' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
{{Sandbox_Reserved_510042_1}}
{{Sandbox_Reserved_510042_1}}
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->

Revision as of 10:50, 13 May 2014

Insert caption here

Drag the structure with the mouse to rotate
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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


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). 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

Drag the structure with the mouse to rotate

Additional Information

References

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_940"
Personal tools