2LGW

Solution Structure of the J Domain of HSJ1a

2LGW の概要

• エントリーDOI: 10.2210/pdb2lgw/pdb
• 関連するPDBエントリー: 2LMG
• NMR情報: BMRB: 17825
• 分子名称: DnaJ homolog subfamily B member 2 (1 entity in total)
• 機能のキーワード: j domain, hsj1a, co-chaperon, chaperone
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11297.48

構造登録者

Zhou, C.,Gao, X.,Cao, C.,Hu, H. (登録日: 2011-08-02, 公開日: 2012-01-11, 最終更新日: 2024-05-15)

主引用文献

Gao, X.C.,Zhou, C.J.,Zhou, Z.R.,Wu, M.,Cao, C.Y.,Hu, H.Y.
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.
J.Biol.Chem., 287:6044-6052, 2012

PubMed Abstract: The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding β-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical α-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones.

PubMed: 22219199
DOI: 10.1074/jbc.M111.294728

実験手法

SOLUTION NMR