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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. 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.
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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 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.
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===Active site organisation===
===Active site organisation===
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The active site of BamB are found in <scene name='57/579710/3q7m_-_interactive_site/2'>BamB interactive sites </scene>.
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The active site of BamB are found in <scene name='57/579710/3q7m_-_interactive_site/2'>BamB interactive sites </scene>. Both electronegative (E197, D246, D248, D288, D303, E370) and interactive residues of IL4 and IL5 (L192, L194, R195,D246 and D248) are found at the hole / center of the beta barrel region. This region is electronegative due to its electronegative residues around this region. The R195 of IL4 is responsible for the salt bridge formation with the D241 of PORTA 3 region of BamA protein.

Revision as of 17:17, 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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