3d2f: Difference between revisions
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==Crystal structure of a complex of Sse1p and Hsp70== | ==Crystal structure of a complex of Sse1p and Hsp70== | ||
<StructureSection load='3d2f' size='340' side='right' caption='[[3d2f]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3d2f' size='340' side='right' caption='[[3d2f]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2e|3d2e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2e|3d2e]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSE1, MSI3, YPL106C, LPG3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSE1, MSI3, YPL106C, LPG3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3d2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2f OCA], [http://pdbe.org/3d2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d2f RCSB], [http://www.ebi.ac.uk/pdbsum/3d2f 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=3d2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2f OCA], [http://pdbe.org/3d2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d2f RCSB], [http://www.ebi.ac.uk/pdbsum/3d2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3d2f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3d2f" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:07, 16 November 2017
Crystal structure of a complex of Sse1p and Hsp70Crystal structure of a complex of Sse1p and Hsp70
Structural highlights
Function[HSP7F_YEAST] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein folding by Hsp70 is tightly controlled by cochaperones, including J-domain proteins that trigger ATP hydrolysis and nucleotide exchange factors (NEFs) that remove ADP from Hsp70. Here we present the crystal structure of the yeast NEF Sse1p (Hsp110) in complex with the nucleotide-binding domain (NBD) of Hsp70. Hsp110 proteins are homologous to Hsp70s and consist of an NBD, a beta sandwich domain, and a three helix bundle domain (3HBD). In the complex, the NBD of Sse1p is ATP bound, and together with the 3HBD it embraces the NBD of Hsp70, inducing opening and the release of bound ADP from Hsp70. Mutations that abolish NEF activity are lethal, thus defining nucleotide exchange on Hsp70 as an essential function of Sse1p. Our data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.,Polier S, Dragovic Z, Hartl FU, Bracher A Cell. 2008 Jun 13;133(6):1068-79. PMID:18555782[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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