Sandbox Reserved 940
From Proteopedia
| Line 8: | Line 8: | ||
===Overview=== | ===Overview=== | ||
| - | 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'''). | + | 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. 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> | ||
===Interactions with other molecules=== | ===Interactions with other molecules=== | ||
| - | Close up picture, with explanation what we see | + | BamB interact with BamA through residues L192, L194, R195, D246, and D248.These residues are found on IL4 ( L192, L194, R195) and IL5 (D246, D248). BamB interacts with the PORTA 2-4 regions of BamA. The IL4 of the The BamB (R195)protein interact with the PORTA 3 regions of the BamA (D241)region by forming a salt bridge. interact with the Close up picture, with explanation what we see |
===Active site organisation=== | ===Active site organisation=== | ||
| - | BamB | + | The active site of BamB are found in IL4 (L192, L194, R195) and IL5(D246, and D248). |
Revision as of 00:10, 15 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 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
| |||||||||||
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
