3A8Y

Crystal structure of the complex between the BAG5 BD5 and Hsp70 NBD

3A8Y の概要

• エントリーDOI: 10.2210/pdb3a8y/pdb
• 分子名称: Heat shock 70 kDa protein 1, BAG family molecular chaperone regulator 5, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: bag domain, hsp70, atpase domain, protein complex, triple helix, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P08107
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118886.37

構造登録者

Arakawa, A.,Handa, N.,Ohsawa, N.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2009-10-13, 公開日: 2010-03-31, 最終更新日: 2024-10-16)

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

X-RAY DIFFRACTION (2.3 Å)