View source for 2lsv


==The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail==
<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LSV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [https://pdbe.org/2lsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [https://www.ebi.ac.uk/pdbsum/2lsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lsv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TAH1_YEAST TAH1_YEAST] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase assembly through interaction with the R2TP complex. This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP. Its minimal TPR domain includes two TPR motifs and a capping helix. We established the high-resolution solution structures of Tah1 free and in complex with the Hsp90 C-terminal peptide. The TPR fold is similar in the free and bound forms and we show experimentally that in addition to its solvating/stabilizing role, the capping helix is essential for the recognition of the Hsp90 704EMEEVD709 motif. In addition to Lys79 and Arg83 from the carboxylate clamp, this helix bears Tyr82 forming a pi/S-CH3 interaction with Hsp90 M705 from the peptide 310 helix. The Tah1 C-terminal region is unfolded, and we demonstrate that it is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding.

High-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex.,Back R, Dominguez C, Rothe B, Bobo C, Beaufils C, Morera S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X Structure. 2013 Sep 4. pii: S0969-2126(13)00296-7. doi:, 10.1016/j.str.2013.07.024. PMID:24012479<ref>PMID:24012479</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lsv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Allain F]]
[[Category: Back R]]
[[Category: Beaufils C]]
[[Category: Bobo C]]
[[Category: Branlant C]]
[[Category: Charpentier B]]
[[Category: Dominguez C]]
[[Category: Manival X]]
[[Category: Meyer P]]
[[Category: Morera S]]
[[Category: Rothe B]]