5NRO

Structure of full-length DnaK with bound J-domain

5NRO の概要

• エントリーDOI: 10.2210/pdb5nro/pdb
• 分子名称: Chaperone protein DnaK, Chaperone protein DnaJ, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: dnak, dnaj, chaperone, hsp70, hsp40
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P0A6Y8 P08622
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78843.51

構造登録者

Kopp, J.,Kityk, R.,Mayer, M.P. (登録日: 2017-04-25, 公開日: 2018-01-17, 最終更新日: 2024-11-06)

主引用文献

Kityk, R.,Kopp, J.,Mayer, M.P.
Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones.
Mol. Cell, 69:227-237.e4, 2018

PubMed Abstract: Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and concomitant substrate trapping. We present the crystal structure of the J-domain of Escherichia coli DnaJ in complex with the E. coli Hsp70 DnaK. The J-domain interacts not only with DnaK's nucleotide-binding domain (NBD) but also with its substrate-binding domain (SBD) and packs against the highly conserved interdomain linker. Mutational replacement of contacts between J-domain and SBD strongly reduces the ability of substrates to stimulate ATP hydrolysis in the presence of DnaJ and compromises viability at heat shock temperatures. Our data demonstrate that the J-domain and the substrate do not deliver completely independent signals for ATP hydrolysis, but the J-domain, in addition to its direct influence on Hsp70s catalytic center, makes Hsp70 more responsive for the hydrolysis-inducing signal of the substrate, resulting in efficient substrate trapping.

PubMed: 29290615
DOI: 10.1016/j.molcel.2017.12.003

実験手法

X-RAY DIFFRACTION (3.25 Å)