View source for 8qpv


==Handover Complex: BAM bound OmpX and extended SurA==
<StructureSection load='8qpv' size='340' side='right'caption='[[8qpv]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qpv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QPV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qpv OCA], [https://pdbe.org/8qpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qpv RCSB], [https://www.ebi.ac.uk/pdbsum/8qpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qpv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BAMA_ECOLI BAMA_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded beta-barrel assembly machinery (BAM). Unfolded OMPs are delivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP delivery and folding remains unclear. Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM structures of a series of complexes. The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may trigger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM lateral gate for insertion into the outer membrane. Mutations that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporting the key role of SurA in outer membrane biogenesis.

Outer membrane protein assembly mediated by BAM-SurA complexes.,Fenn KL, Horne JE, Crossley JA, Bohringer N, Horne RJ, Schaberle TF, Calabrese AN, Radford SE, Ranson NA Nat Commun. 2024 Sep 1;15(1):7612. doi: 10.1038/s41467-024-51358-x. PMID:39218969<ref>PMID:39218969</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qpv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Fenn KL]]
[[Category: Ranson NA]]