2O1V

Structure of full length GRP94 with ADP bound

2O1V の概要

• エントリーDOI: 10.2210/pdb2o1v/pdb
• 関連するPDBエントリー: 1TC6 2O1T 2O1U 2O1W
• 分子名称: Endoplasmin, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: grp94, hsp82, hsp90, htpg, chaperone, adp, gp96, endoplasmin
• 由来する生物種: Canis lupus familiaris (dog); 詳細
• 細胞内の位置: Endoplasmic reticulum lumen: P41148
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 154143.65

構造登録者

Dollins, D.E.,Warren, J.J.,Immormino, R.M.,Gewirth, D.T. (登録日: 2006-11-29, 公開日: 2007-10-23, 最終更新日: 2023-12-27)

主引用文献

Dollins, D.E.,Warren, J.J.,Immormino, R.M.,Gewirth, D.T.
Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones.
Mol.Cell, 28:41-56, 2007

PubMed Abstract: GRP94, an essential endoplasmic reticulum chaperone, is required for the conformational maturation of proteins destined for cell-surface display or export. The extent to which GRP94 and its cytosolic paralog, Hsp90, share a common mechanism remains controversial. GRP94 has not been shown conclusively to hydrolyze ATP or bind cochaperones, and both activities, by contrast, result in conformational changes and N-terminal dimerization in Hsp90 that are critical for its function. Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP. The chaperone is conformationally insensitive to the identity of the bound nucleotide, adopting a "twisted V" conformation that precludes N-terminal domain dimerization. We also present conclusive evidence that GRP94 possesses ATPase activity. Our observations provide a structural explanation for GRP94's observed rate of ATP hydrolysis and suggest a model for the role of ATP binding and hydrolysis in the GRP94 chaperone cycle.

PubMed: 17936703
DOI: 10.1016/j.molcel.2007.08.024

実験手法

X-RAY DIFFRACTION (2.45 Å)