7RAX
ATP-binding state of the nucleotide-binding domain of Hsp70 DnaK mutant T199A
Summary for 7RAX
| Entry DOI | 10.2210/pdb7rax/pdb |
| Descriptor | Chaperone protein DnaK, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | molecular chaperone, hsp70, protein folding, chaperone |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 43236.80 |
| Authors | Wang, W.,Hendrickson, W.A. (deposition date: 2021-07-04, release date: 2023-07-05, Last modification date: 2024-10-09) |
| Primary citation | Wang, W.,Liu, Q.,Liu, Q.,Hendrickson, W.A. Conformational equilibria in allosteric control of Hsp70 chaperones. Mol.Cell, 81:3919-3933.e7, 2021 Cited by PubMed Abstract: 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, Hsp70-ATP, restricts ATP hydrolysis and binds peptides poorly, whereas a stimulating state, Hsp70-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. PubMed: 34453889DOI: 10.1016/j.molcel.2021.07.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.41 Å) |
Structure validation
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