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2lsv

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==The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail==
==The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail==
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<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lsu|2lsu]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<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>
<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>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:17114002</ref>
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[https://www.uniprot.org/uniprot/TAH1_YEAST TAH1_YEAST]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Allain, F]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Back, R]]
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[[Category: Allain F]]
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[[Category: Beaufils, C]]
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[[Category: Back R]]
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[[Category: Bobo, C]]
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[[Category: Beaufils C]]
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[[Category: Branlant, C]]
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[[Category: Bobo C]]
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[[Category: Charpentier, B]]
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[[Category: Branlant C]]
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[[Category: Dominguez, C]]
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[[Category: Charpentier B]]
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[[Category: Manival, X]]
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[[Category: Dominguez C]]
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[[Category: Meyer, P]]
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[[Category: Manival X]]
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[[Category: Morera, S]]
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[[Category: Meyer P]]
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[[Category: Rothe, B]]
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[[Category: Morera S]]
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[[Category: Chaperone-binding protein-chaperone complex]]
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[[Category: Rothe B]]

Current revision

The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail

PDB ID 2lsv

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