View source for 25fq


==BAM-SurA complex (Core only)==
<StructureSection load='25fq' size='340' side='right'caption='[[25fq]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[25fq]] 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=25FQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=25FQ 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]] 3.6&#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=25fq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=25fq OCA], [https://pdbe.org/25fq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=25fq RCSB], [https://www.ebi.ac.uk/pdbsum/25fq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=25fq 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][https://www.uniprot.org/uniprot/SURA_ECO57 SURA_ECO57] Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outer membrane (OM) of Gram-negative bacteria acts as a permeability barrier against toxic compounds. Its integrity is maintained by various outer membrane proteins (OMPs), which are inserted into the OM by the beta-barrel assembly machinery (BAM) complex. The periplasmic chaperone SurA delivers unfolded OMPs to BAM; however, the mechanism of substrate transfer remains unclear. Here, we show that the flexible P1 and P2 domains of SurA regulate the function of its Core domain and interact with BAM components, including BamE, whose interaction with the P2 domain is crucial for efficient OMP assembly. Moreover, cryo-electron microscopy reveals four distinct Escherichia coli SurA-BAM structures, suggesting dynamic domain rearrangements of SurA. Based on these findings, we propose a dynamic model in which SurA transfers substrates to BAM through multiple conformational changes, providing a unified framework for chaperone-assisted OMP biogenesis.

Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.,Miyazaki R, Kohga H, Matsuoka N, Maruno Y, Yoshimoto W, Takahashi YS, Yanto DHY, Nugraha Y, Shigematsu H, Shiota T, Tsukazaki T Nat Commun. 2026 Sep 4;17(1):9061. doi: 10.1038/s41467-026-76843-3. PMID:42697891<ref>PMID:42697891</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 25fq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Kohga H]]
[[Category: Miyazaki R]]
[[Category: Tsukazaki T]]