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7KRT

Restraining state of a truncated Hsp70 DnaK

7KRT の概要
エントリーDOI10.2210/pdb7krt/pdb
関連するPDBエントリー7KO2
分子名称Chaperone protein DnaK, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
機能のキーワードmolecular chaperone, hsp70, protein folding, chaperone
由来する生物種Escherichia coli (strain K12)
タンパク質・核酸の鎖数4
化学式量合計262111.62
構造登録者
Wang, W.,Hendrickson, W.A. (登録日: 2020-11-20, 公開日: 2021-09-15, 最終更新日: 2024-11-13)
主引用文献Wang, W.,Liu, Q.,Liu, Q.,Hendrickson, W.A.
Conformational equilibria in allosteric control of Hsp70 chaperones.
Mol.Cell, 81:3919-, 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: 34453889
DOI: 10.1016/j.molcel.2021.07.039
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.79 Å)
構造検証レポート
Validation report summary of 7krt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-01-15に公開中

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