4B9Q

Open conformation of ATP-bound Hsp70 homolog DnaK

4B9Q の概要

• エントリーDOI: 10.2210/pdb4b9q/pdb
• 関連するPDBエントリー: 1BPR 1DG4 1DKG 1DKX 1DKY 1DKZ 1Q5L 2BPR
• 分子名称: CHAPERONE PROTEIN DNAK, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: chaperone
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 267199.79

構造登録者

Kopp, J.,Mayer, M.P.,Sinning, I. (登録日: 2012-09-06, 公開日: 2012-11-14, 最終更新日: 2024-11-06)

主引用文献

Kityk, R.,Kopp, J.,Sinning, I.,Mayer, M.P.
Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
Mol.Cell, 48:863-, 2012

PubMed Abstract: Central to the chaperone function of Hsp70s is the transition between open and closed conformations of their polypeptide substrate binding domain (SBD), which is regulated through an allosteric mechanism via ATP binding and hydrolysis in their nucleotide binding domain (NBD). Although the structure of the closed conformation of Hsp70s is well studied, the open conformation has remained elusive. Here, we report on the 2.4 Å crystal structure of the ATP-bound open conformation of the Escherichia coli Hsp70 homolog DnaK. In the open DnaK structure, the β sheet and α-helical lid subdomains of the SBD are detached from one another and docked to different faces of the NBD. The contacts between the β sheet subdomain and the NBD reveal the mechanism of allosteric regulation. In addition, we demonstrate that docking of the β sheet and α-helical lid subdomains to the NBD is a sequential process influenced by peptide and protein substrates.

PubMed: 23123194
DOI: 10.1016/J.MOLCEL.2012.09.023

実験手法

X-RAY DIFFRACTION (2.4 Å)