7NDX

Crystal structure of the human HSP40 DNAJB1-CTDs in complex with a peptide of NudC

7NDX の概要

• エントリーDOI: 10.2210/pdb7ndx/pdb
• 分子名称: DnaJ homolog subfamily B member 1, Nuclear migration protein nudC, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: chaperones, protein complex, chaperone
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25810.68

構造登録者

Delhommel, F.,Zak, K.M.,Popowicz, G.M.,Sattler, M. (登録日: 2021-02-02, 公開日: 2022-01-19, 最終更新日: 2024-01-31)

主引用文献

Biebl, M.M.,Delhommel, F.,Faust, O.,Zak, K.M.,Agam, G.,Guo, X.,Muhlhofer, M.,Dahiya, V.,Hillebrand, D.,Popowicz, G.M.,Kampmann, M.,Lamb, D.C.,Rosenzweig, R.,Sattler, M.,Buchner, J.
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems.
Mol.Cell, 82:555-, 2022

PubMed Abstract: In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem with the maturation of a diverse array of client proteins. The transfer of nonnative clients between these systems is essential to the chaperoning process, but how it is regulated is still not clear. We discovered that NudC is an essential transfer factor with an unprecedented mode of action: NudC interacts with Hsp40 in Hsp40-Hsp70-client complexes and displaces Hsp70. Then, the interaction of NudC with Hsp90 allows the direct transfer of Hsp40-bound clients to Hsp90 for further processing. Consistent with this mechanism, NudC increases client activation in vitro as well as in cells and is essential for cellular viability. Together, our results show the complexity of the cooperation between the major chaperone machineries in the eukaryotic cytosol.

PubMed: 35063133
DOI: 10.1016/j.molcel.2021.12.031

実験手法

X-RAY DIFFRACTION (2.541 Å)