2lsv - Revision history

OCA at 05:51, 15 May 2024

OCA — Wed, 15 May 2024 05:51:22 GMT

←Older revision		Revision as of 05:51, 15 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== 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>		<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='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>	+	</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>		</table>
	== Function ==		== Function ==

OCA at 13:08, 22 February 2023

OCA — Wed, 22 Feb 2023 13:08:34 GMT

←Older revision		Revision as of 13:08, 22 February 2023
Line 1:		Line 1:

	==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==
-	<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<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='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>~~	+	</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>
-	<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>	+
-	<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 ==
-	[[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>	+	[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 ==
Line 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Allain, F]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Back, R]]	+	[[Category: Allain F]]
-	[[Category: Beaufils, C]]	+	[[Category: Back R]]
-	[[Category: Bobo, C]]	+	[[Category: Beaufils C]]
-	[[Category: Branlant, C]]	+	[[Category: Bobo C]]
-	[[Category: Charpentier, B]]	+	[[Category: Branlant C]]
-	[[Category: Dominguez, C]]	+	[[Category: Charpentier B]]
-	[[Category: Manival, X]]	+	[[Category: Dominguez C]]
-	[[Category: Meyer, P]]	+	[[Category: Manival X]]
-	[[Category: Morera, S]]	+	[[Category: Meyer P]]
-	[[Category: Rothe, B]]	+	[[Category: Morera S]]
-	~~[[Category: Chaperone-binding protein-chaperone complex~~]]	+	[[Category: Rothe B]]

OCA at 10:52, 19 May 2021

OCA — Wed, 19 May 2021 10:52:29 GMT

←Older revision		Revision as of 10:52, 19 May 2021
Line 1:		Line 1:

	==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==
-	<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2lsv' size='340' side='right'caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [~~http~~://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 [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2LSV FirstGlance]. <br>	+	<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>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>	+	</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>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+	<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>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [~~http~~://pdbe.org/2lsv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2lsv PDBsum], [~~http~~://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 ==
-	[[~~http~~://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>	+	[[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Baker's yeast]]		[[Category: Baker's yeast]]
		+	[[Category: Large Structures]]
	[[Category: Allain, F]]		[[Category: Allain, F]]
	[[Category: Back, R]]		[[Category: Back, R]]

OCA at 20:10, 1 August 2018

OCA — Wed, 01 Aug 2018 20:10:01 GMT

←Older revision		Revision as of 20:10, 1 August 2018
Line 1:		Line 1:
		+
	==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==
	<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [http://pdbe.org/2lsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [http://www.ebi.ac.uk/pdbsum/2lsv PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [http://pdbe.org/2lsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [http://www.ebi.ac.uk/pdbsum/2lsv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lsv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 16:27, 11 September 2015

OCA — Fri, 11 Sep 2015 16:27:36 GMT

←Older revision		Revision as of 16:27, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LSV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LSV FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [http://www.ebi.ac.uk/pdbsum/2lsv PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [http://pdbe.org/2lsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [http://www.ebi.ac.uk/pdbsum/2lsv PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2lsv" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae s288c~~]]	+	[[Category: Baker's yeast]]
	[[Category: Allain, F]]		[[Category: Allain, F]]
	[[Category: Back, R]]		[[Category: Back, R]]

OCA at 19:00, 25 December 2014

OCA — Thu, 25 Dec 2014 19:00:06 GMT

←Older revision		Revision as of 19:00, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2lsv\| PDB=2lsv \| SCENE= }}~~	+	==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===	+	<StructureSection load='2lsv' size='340' side='right' caption='[[2lsv]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_24012479}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2lsv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LSV FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2lsu\|2lsu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TAH1, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lsv RCSB], [http://www.ebi.ac.uk/pdbsum/2lsv PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://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>		[[http://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>
		+	<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.

-	~~==About this~~ Structure==	+	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>
-	~~[[2lsv]] is a 2 chain structure with sequence from [http://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]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024012479</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
-	[[Category: Allain, F.]]	+	[[Category: Allain, F]]
-	[[Category: Back, R.]]	+	[[Category: Back, R]]
-	[[Category: Beaufils, C.]]	+	[[Category: Beaufils, C]]
-	[[Category: Bobo, C.]]	+	[[Category: Bobo, C]]
-	[[Category: Branlant, C.]]	+	[[Category: Branlant, C]]
-	[[Category: Charpentier, B.]]	+	[[Category: Charpentier, B]]
-	[[Category: Dominguez, C.]]	+	[[Category: Dominguez, C]]
-	[[Category: Manival, X.]]	+	[[Category: Manival, X]]
-	[[Category: Meyer, P.]]	+	[[Category: Meyer, P]]
-	[[Category: Morera, S.]]	+	[[Category: Morera, S]]
-	[[Category: Rothe, B.]]	+	[[Category: Rothe, B]]
	[[Category: Chaperone-binding protein-chaperone complex]]		[[Category: Chaperone-binding protein-chaperone complex]]

OCA at 06:19, 2 October 2013

OCA — Wed, 02 Oct 2013 06:19:40 GMT

←Older revision		Revision as of 06:19, 2 October 2013
Line 1:		Line 1:
	{{STRUCTURE_2lsv\| PDB=2lsv \| SCENE= }}		{{STRUCTURE_2lsv\| PDB=2lsv \| SCENE= }}
	===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===
		+	{{ABSTRACT_PUBMED_24012479}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024012479</ref><references group="xtra"/><references/>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Allain, F.]]		[[Category: Allain, F.]]

OCA at 06:21, 20 June 2013

OCA — Thu, 20 Jun 2013 06:21:58 GMT

←Older revision		Revision as of 06:21, 20 June 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_2lsv\| PDB=2lsv \| SCENE= }}
		+	===The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail===

-	The ~~entry 2lsv~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://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>

-	~~Authors~~: ~~Back, R~~.~~, Dominguez, C~~.~~, Rothe, B~~.~~, Bobo, C., Beaufils, C., Morera, S., Meyer, P., Charpentier, B~~.~~, Branlant, C~~.~~, Allain, F~~.~~, Manival, X~~.	+	==About this Structure==
		+	[[2lsv]] is a 2 chain structure with sequence from [http://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].

-	~~Description~~: ~~The NMR high resolution structure of yeast Tah1 in complex with the Hsp90~~ C-~~terminal tail~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[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.]]
		+	[[Category: Chaperone-binding protein-chaperone complex]]

OCA at 05:12, 30 May 2012

OCA — Wed, 30 May 2012 05:12:37 GMT

←Older revision		Revision as of 05:12, 30 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2lsv is ON HOLD	+	The entry 2lsv is ON HOLD until Paper Publication

	Authors: Back, R., Dominguez, C., Rothe, B., Bobo, C., Beaufils, C., Morera, S., Meyer, P., Charpentier, B., Branlant, C., Allain, F., Manival, X.		Authors: Back, R., Dominguez, C., Rothe, B., Bobo, C., Beaufils, C., Morera, S., Meyer, P., Charpentier, B., Branlant, C., Allain, F., Manival, X.

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

OCA: Protected "2lsv" [edit=sysop:move=sysop]

OCA — Wed, 16 May 2012 08:32:50 GMT

Protected "2lsv" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:32, 16 May 2012