View source for 8bvq


==E. coli BAM complex (BamABCDE) bound to darobactin B==
<StructureSection load='8bvq' size='340' side='right'caption='[[8bvq]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bvq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Photorhabdus_heterorhabditis Photorhabdus heterorhabditis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BVQ 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UX8:(2~{S},3~{R})-2-azanyl-3-(1~{H}-indol-3-yl)-3-oxidanyl-propanoic+acid'>UX8</scene></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=8bvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bvq OCA], [https://pdbe.org/8bvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bvq RCSB], [https://www.ebi.ac.uk/pdbsum/8bvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bvq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BAME_ECOLI BAME_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.<ref>PMID:17404237</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> <ref>PMID:21207987</ref> <ref>PMID:21586578</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The beta-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment.

Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.,Haysom SF, Machin J, Whitehouse JM, Horne JE, Fenn K, Ma Y, El Mkami H, Bohringer N, Schaberle TF, Ranson NA, Radford SE, Pliotas C Angew Chem Int Ed Engl. 2023 May 10:e202218783. doi: 10.1002/anie.202218783. PMID:37162386<ref>PMID:37162386</ref>

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