Sandbox Reserved 940

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===Overview===
===Overview===
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The native ''E. coli'' BamB structure contains residues 21–392 arranged as an <scene name='57/579710/Eight_blades_of_beta-barrel/1'> eight bladed β-barrel</scene> with hole at the center. Each blade is connected by interconnected loop ('''IL'''). BamB is strongly electronegative at the center at either side of the hole due to the presence of strong <scene name='57/579710/Elecronegative_bamb_part/1'>electronegative</scene> residues in these regions (E197, D246, D248, D288, D303, E370). Among the ILs, IL4 and IL5 are either partially or completely disordered. This helps the BamB to interact with the BamA. Moreover, the interacting residues are found in these loops. How the overall structure looks like? Subunits orientation, chains: the number and relative positions, etc.
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The native ''E. coli'' BamB structure contains residues 21–392 arranged as an eight bladed <scene name='57/579710/Eight_blades_of_beta-barrel/1'> eight bladed β-barrel</scene> with hole at the center. Each blade is connected by interconnected loop ('''IL'''). BamB is strongly electronegative at the center at either side of the hole due to the presence of strong <scene name='57/579710/Elecronegative_bamb_part/1'>electronegative</scene> residues in these regions (E197, D246, D248, D288, D303, E370). Among the ILs, IL4 and IL5 are either partially or completely disordered. This helps the BamB to interact with the BamA. Moreover, the interacting residues are found in these loops. How the overall structure looks like? Subunits orientation, chains: the number and relative positions, etc.
Here is the
Here is the
<scene name='57/579693/Overall_chain/1'>rainbow representation</scene> of the main chain of lysozyme. And here is the <scene name='57/579693/Alpha_helix/1'>helical representation</scene> of the same lysozyme molecule. <scene name='57/579693/3htc-1/1'>whatever you want!</scene>
<scene name='57/579693/Overall_chain/1'>rainbow representation</scene> of the main chain of lysozyme. And here is the <scene name='57/579693/Alpha_helix/1'>helical representation</scene> of the same lysozyme molecule. <scene name='57/579693/3htc-1/1'>whatever you want!</scene>

Revision as of 20:00, 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

Escherichia coli BamB structure (PDB entry 3Q7M)

Drag the structure with the mouse to rotate

Additional Information

References

‘
  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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