14GS

GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1

14GS の概要

• エントリーDOI: 10.2210/pdb14gs/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: transferase, apoenzyme, detoxification
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P09211
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47146.01

構造登録者

Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W. (登録日: 1997-11-29, 公開日: 1999-01-13, 最終更新日: 2024-05-22)

主引用文献

Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W.
Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
Biochemistry, 37:9912-9917, 1998

PubMed Abstract: Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.

PubMed: 9665696
DOI: 10.1021/bi980323w

実験手法

X-RAY DIFFRACTION (2.8 Å)