7n46
From Proteopedia
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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=7n46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n46 OCA], [https://pdbe.org/7n46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n46 RCSB], [https://www.ebi.ac.uk/pdbsum/7n46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n46 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=7n46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n46 OCA], [https://pdbe.org/7n46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n46 RCSB], [https://www.ebi.ac.uk/pdbsum/7n46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n46 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Heat-shock proteins of 70 kDa (Hsp70s) are vital for all life and are notably important in protein folding. Hsp70s use ATP binding and hydrolysis at a nucleotide-binding domain (NBD) to control the binding and release of client polypeptides at a substrate-binding domain (SBD); however, the mechanistic basis for this allostery has been elusive. Here, we first characterize biochemical properties of selected domain-interface mutants in bacterial Hsp70 DnaK. We then develop a theoretical model for allosteric equilibria among Hsp70 conformational states to explain the observations: a restraining state, Hsp70R-ATP, restricts ATP hydrolysis and binds peptides poorly, whereas a stimulating state, Hsp70S-ATP, hydrolyzes ATP rapidly and has high intrinsic substrate affinity but rapid binding kinetics. We support this model for allosteric regulation with DnaK structures obtained in the postulated stimulating state S with biochemical tests of the S-state interface and with improved peptide-binding-site definition in an R-state structure. | ||
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| + | Conformational equilibria in allosteric control of Hsp70 chaperones.,Wang W, Liu Q, Liu Q, Hendrickson WA Mol Cell. 2021 Aug 26. pii: S1097-2765(21)00623-7. doi:, 10.1016/j.molcel.2021.07.039. PMID:34453889<ref>PMID:34453889</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7n46" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
ADP-binding state of the nucleotide-binding domain of Hsp70 DnaK
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