View source for 8k2s


==The structure of HtpG M domain in complex with unstructured D131D binding site a==
<StructureSection load='8k2s' size='340' side='right'caption='[[8k2s]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8k2s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8K2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8K2S FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=8k2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8k2s OCA], [https://pdbe.org/8k2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8k2s RCSB], [https://www.ebi.ac.uk/pdbsum/8k2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8k2s ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A7A6VTW3_ECOLX A0A7A6VTW3_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Molecular chaperone heat shock protein 90 (Hsp90) is a ubiquitous regulator that fine-tunes and remodels diverse client proteins, exerting profound effects on normal biology and diseases. Unraveling the mechanistic details of Hsp90's function requires atomic-level insights into its client interactions throughout the adenosine triphosphate-coupled functional cycle. However, the structural details of the initial encounter complex in the chaperone cycle, wherein Hsp90 adopts an open conformation while engaging with the client, remain elusive. Here, using nuclear magnetic resonance spectroscopy, we determined the solution structure of Hsp90 in its open state, bound to a disordered client. Our findings reveal that Hsp90 uses two distinct binding sites, collaborating synergistically to capture discrete hydrophobic segments within client proteins. This bipartite interaction generates a versatile complex that facilitates rapid conformational sampling. Moreover, our investigations spanning various clients and Hsp90 orthologs demonstrate a pervasive mechanism used by Hsp90 orthologs to accommodate the vast array of client proteins. Collectively, our work contributes to establish a unified conceptual and mechanistic framework, elucidating the intricate interplay between Hsp90 and its clients.

Structural basis for the dynamic chaperoning of disordered clients by Hsp90.,Qu X, Zhao S, Wan C, Zhu L, Ji T, Rossi P, Wang J, Kalodimos CG, Wang C, Xu W, Huang C Nat Struct Mol Biol. 2024 Jun 18. doi: 10.1038/s41594-024-01337-z. PMID:38890550<ref>PMID:38890550</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Huang C]]
[[Category: Qu X]]