Sandbox Reserved 940
From Proteopedia
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==Structure== | ==Structure== | ||
<Structure load='3Q7M' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='3Q7M' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
| - | + | The native ''E. coli'' BamB structure contains residues 21–392 arranged as an eight-bladed β-propeller 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 electronegative residues in these regions (E197, D246, D248, D288, D303, E370). Among the ILs, IL4 and IL5 are unordered and the interacting residues are found in these loops. | |
Anything in this section will appear adjacent to the 3D structure and will be scrollable. | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
===Overview=== | ===Overview=== | ||
Revision as of 21:44, 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
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The native E. coli BamB structure contains residues 21–392 arranged as an eight-bladed β-propeller 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 electronegative residues in these regions (E197, D246, D248, D288, D303, E370). Among the ILs, IL4 and IL5 are unordered and the interacting residues are found in these loops. Anything in this section will appear adjacent to the 3D structure and will be scrollable.
Overview
How the overall structure looks like? Subunits orientation, chains: the number and relative positions, etc. Here is the of the main chain of lysozyme. And here is the of the same lysozyme molecule.
Interactions with other molecules
Close up picture, with explanation what we see
Active site organisation
Conclusions
</StructureSection>
Additional Information
References
‘- ↑ 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
