2D9D

Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5

2D9D の概要

• エントリーDOI: 10.2210/pdb2d9d/pdb
• 分子名称: BAG family molecular chaperone regulator 5 (1 entity in total)
• 機能のキーワード: triple helix bundle, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, 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: 9842.25

構造登録者

Hatta, R.,Hayashi, F.,Yoshida, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-12-09, 公開日: 2006-12-09, 最終更新日: 2024-05-29)

主引用文献

Arakawa, A.,Handa, N.,Ohsawa, N.,Shida, M.,Kigawa, T.,Hayashi, F.,Shirouzu, M.,Yokoyama, S.
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
Structure, 18:309-319, 2010

PubMed Abstract: ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.

PubMed: 20223214
DOI: 10.1016/j.str.2010.01.004

実験手法

SOLUTION NMR