6PQ2

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

6PQ2 の概要

• エントリーDOI: 10.2210/pdb6pq2/pdb
• 関連するPDBエントリー: 6ppt
• NMR情報: BMRB: 30628
• 分子名称: Alkaline phosphatase,Chaperone DnaJ domain-containing protein fusion (1 entity in total)
• 機能のキーワード: client recognition, chaperone
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9256.69

構造登録者

Jiang, Y.,Rossi, P.,Kalodimos, C.G. (登録日: 2019-07-08, 公開日: 2019-09-18, 最終更新日: 2024-05-01)

主引用文献

Jiang, Y.,Rossi, P.,Kalodimos, C.G.
Structural basis for client recognition and activity of Hsp40 chaperones.
Science, 365:1313-1319, 2019

PubMed Abstract: Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release.

PubMed: 31604242
DOI: 10.1126/science.aax1280

実験手法

SOLUTION NMR