1YNS

Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

1YNS の概要

• エントリーDOI: 10.2210/pdb1yns/pdb
• 関連するPDBエントリー: 1WDH
• 分子名称: E-1 enzyme, MAGNESIUM ION, 2-OXOHEPTYLPHOSPHONIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase fold, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q9UHY7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29228.68

構造登録者

Wang, H.,Pang, H.,Bartlam, M.,Rao, Z. (登録日: 2005-01-25, 公開日: 2005-05-17, 最終更新日: 2024-03-13)

主引用文献

Wang, H.,Pang, H.,Bartlam, M.,Rao, Z.
Crystal structure of human e1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase
J.Mol.Biol., 348:917-926, 2005

PubMed Abstract: Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively. The structures support the proposed mechanism of phosphatase activity and further suggest the probable mechanism of enolization. We establish a model for substrate binding to describe in detail the enzymatic reaction and the formation of the transition state, which will provide insight into the reaction mechanisms of other enzymes in the same family.

PubMed: 15843022
DOI: 10.1016/j.jmb.2005.01.072

実験手法

X-RAY DIFFRACTION (1.7 Å)