1TC6

Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex

1TC6 の概要

• エントリーDOI: 10.2210/pdb1tc6/pdb
• 関連するPDBエントリー: 1QY5 1QY8 1QYE 1QYH 1TBW 1TC0
• 分子名称: Endoplasmin, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: grp94, hsp90, adp, bergerat, chaperone, endoplasmic reticulum
• 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: 54902.17

構造登録者

Gewirth, D.T.,Immormino, R.M.,Dollins, D.E.,Shaffer, P.L.,Walker, M.A.,Soldano, K.L. (登録日: 2004-05-20, 公開日: 2004-08-24, 最終更新日: 2024-02-14)

主引用文献

Immormino, R.M.,Dollins, D.E.,Shaffer, P.L.,Soldano, K.L.,Walker, M.A.,Gewirth, D.T.
Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone.
J.Biol.Chem., 279:46162-46171, 2004

PubMed Abstract: GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.

PubMed: 15292259
DOI: 10.1074/jbc.M405253200

実験手法

X-RAY DIFFRACTION (1.87 Å)