View source for 28jq


==Poised Complex: BAM bound BepA==
<StructureSection load='28jq' size='340' side='right'caption='[[28jq]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[28jq]] 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=28JQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28JQ 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]] 3.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=28jq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28jq OCA], [https://pdbe.org/28jq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28jq RCSB], [https://www.ebi.ac.uk/pdbsum/28jq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28jq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BAMA_ECO24 BAMA_ECO24] 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.[HAMAP-Rule:MF_01430]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Correct folding of outer membrane proteins (OMPs) by the beta-barrel assembly machinery (BAM) is essential for maintaining the outer membrane (OM) barrier function of diderm bacteria. When OMP biogenesis is perturbed, the beta-barrel assembly enhancing protease A (BepA) binds to BAM to mediate quality control, but how BepA interacts with BAM and degrades substrate OMPs remains unclear. Here, cryoEM structures of BAM-bound BepA reveals that BepA induces large conformational changes in the BAM complex enabling the enzyme to poise its active site within the periplasmic ring of BAM, beneath the BamA barrel. The lid of BepA is dynamic, embedding two of its water-soluble helices deep into the membrane bilayer when BAM-bound, which readies BepA for proteolysis of misfolding OMPs. Movement of BepA's plug is triggered by OMP binding rather than interaction with BAM, activating the enzyme for cleavage. We reveal BepA preferentially recognises Aromatic-X-Aromatic (Ar-X-Ar) motifs which are enriched in OMP sequences. The results reveal a mechanism for proteolytic degradation by BepA in OMP quality control which requires interaction with BAM, the membrane, and its OMP substrates.

BAM-BepA complexes in outer membrane protein quality control.,Fenn KL, Higgins V, Machin JM, Calabrese AN, Berry A, Radford SE, Ranson NA Nat Commun. 2026 Jul 9. doi: 10.1038/s41467-026-75227-x. PMID:42426009<ref>PMID:42426009</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 28jq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Fenn KL]]
[[Category: Ranson NA]]