3IUC

Crystal structure of the human 70kDa heat shock protein 5 (BiP/GRP78) ATPase domain in complex with ADP

3IUC の概要

• エントリーDOI: 10.2210/pdb3iuc/pdb
• 分子名称: Heat shock 70kDa protein 5 (Glucose-regulated protein, 78kDa), ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: helix, structural genomics, structural genomics consortium, sgc, atp-binding, nucleotide-binding, stress response, chaperone
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91422.62

構造登録者

Wisniewska, M.,Karlberg, T.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kallas, A.,Kotyenova, T.,Kotzch, A.,Kraulis, P.,Markova, N.,Moche, M.,Nielsen, T.K.,Nordlund, P.,Nyman, T.,Persson, C.,Roos, A.,Schutz, P.,Siponen, M.I.,Svensson, L.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Wahlberg, E.,Weigelt, J.,Welin, M.,Schuler, H.,Structural Genomics Consortium (SGC) (登録日: 2009-08-31, 公開日: 2009-09-22, 最終更新日: 2023-11-01)

主引用文献

Wisniewska, M.,Karlberg, T.,Lehtio, L.,Johansson, I.,Kotenyova, T.,Moche, M.,Schuler, H.
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78
Plos One, 5:e8625-e8625, 2010

PubMed Abstract: The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) with ATPase activity, and a C-terminal substrate binding domain (SBD). We present the first crystal structures of four human Hsp70 isoforms, those of the NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. As previously with Hsp70 family members, all four proteins crystallized in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB was observed for the HSPA5-ADP complex. The structures presented here support the view that the NBDs of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins.

PubMed: 20072699
DOI: 10.1371/journal.pone.0008625

実験手法

X-RAY DIFFRACTION (2.4 Å)