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7kru
From Proteopedia
(Difference between revisions)
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==Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide== | ==Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide== | ||
| - | <StructureSection load='7kru' size='340' side='right'caption='[[7kru]]' scene=''> | + | <StructureSection load='7kru' size='340' side='right'caption='[[7kru]], [[Resolution|resolution]] 1.82Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KRU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7kru]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KRU 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=7kru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kru OCA], [https://pdbe.org/7kru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kru RCSB], [https://www.ebi.ac.uk/pdbsum/7kru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kru ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7krt|7krt]]</div></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=7kru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kru OCA], [https://pdbe.org/7kru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kru RCSB], [https://www.ebi.ac.uk/pdbsum/7kru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kru ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/A0A6D2W465_ECOLI A0A6D2W465_ECOLI]] Acts as a chaperone.[HAMAP-Rule:MF_00332] | ||
| + | <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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7kru" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hendrickson | + | [[Category: Hendrickson, W A]] |
| - | [[Category: Wang W]] | + | [[Category: Wang, W]] |
| + | [[Category: Chaperone]] | ||
| + | [[Category: Hsp70]] | ||
| + | [[Category: Molecular chaperone]] | ||
| + | [[Category: Protein folding]] | ||
Revision as of 20:14, 20 October 2021
Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide
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