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3uq3

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TPR2AB-domain:pHSP90-complex of yeast Sti1

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 ==TPR2AB-domain:pHSP90-complex of yeast Sti1==
-<StructureSection load='3uq3' size='340' side='right' caption='[[3uq3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='3uq3' size='340' side='right'caption='[[3uq3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uq3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UQ3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uq3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UQ3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3esk|3esk]], [[1elr|1elr]], [[3upv|3upv]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STI1, YOR027W, OR26.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3uq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uq3 OCA], [https://pdbe.org/3uq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uq3 RCSB], [https://www.ebi.ac.uk/pdbsum/3uq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uq3 ProSAT]</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=3uq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uq3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uq3 RCSB], [http://www.ebi.ac.uk/pdbsum/3uq3 PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/STI1_YEAST STI1_YEAST]
-Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the Hsp90 chaperone system in eukaryotes. It binds Hsp70 and Hsp90 simultaneously via TPR (tetratricopeptide repeat) domains. Sti1/Hop contains three TPR domains (TPR1, TPR2A and TPR2B) and two domains of unknown structure (DP1 and DP2). We show that TPR2A is the high affinity Hsp90-binding site and TPR1 and TPR2B bind Hsp70 with moderate affinity. The DP domains exhibit highly homologous alpha-helical folds as determined by NMR. These, and especially DP2, are important for client activation in vivo. The core module of Sti1 for Hsp90 inhibition is the TPR2A-TPR2B segment. In the crystal structure, the two TPR domains are connected via a rigid linker orienting their peptide-binding sites in opposite directions and allowing the simultaneous binding of TPR2A to the Hsp90 C-terminal domain and of TPR2B to Hsp70. Both domains also interact with the Hsp90 middle domain. The accessory TPR1-DP1 module may serve as an Hsp70-client delivery system for the TPR2A-TPR2B-DP2 segment, which is required for client activation in vivo.
-The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.,Schmid AB, Lagleder S, Grawert MA, Rohl A, Hagn F, Wandinger SK, Cox MB, Demmer O, Richter K, Groll M, Kessler H, Buchner J EMBO J. 2012 Jan 6. doi: 10.1038/emboj.2011.472. PMID:22227520<ref>PMID:22227520</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Heat Shock Proteins|Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Large Structures]]
-[[Category: Buchner, J]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Cox, M B]]
+[[Category: Buchner J]]
-[[Category: Demmer, O]]
+[[Category: Cox MB]]
-[[Category: Graewert, M A]]
+[[Category: Demmer O]]
-[[Category: Groll, M]]
+[[Category: Graewert MA]]
-[[Category: Hagn, F]]
+[[Category: Groll M]]
-[[Category: Kessler, H]]
+[[Category: Hagn F]]
-[[Category: Lagleder, S]]
+[[Category: Kessler H]]
-[[Category: Richter, K]]
+[[Category: Lagleder S]]
-[[Category: Roehl, A]]
+[[Category: Richter K]]
-[[Category: Schmid, A B]]
+[[Category: Roehl A]]
-[[Category: Wandinger, S K]]
+[[Category: Schmid AB]]
-[[Category: Chaperone]]
+[[Category: Wandinger SK]]
-[[Category: Hsp90]]
-[[Category: Peptide binding]]

3uq3

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TPR2AB-domain:pHSP90-complex of yeast Sti1

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