5FSE

2.07 A resolution 1,4-Benzoquinone inhibited Sporosarcina pasteurii urease

5FSE の概要

• エントリーDOI: 10.2210/pdb5fse/pdb
• 関連するPDBエントリー: 5FSD
• 分子名称: UREASE SUBUNIT GAMMA, UREASE SUBUNIT BETA, UREASE SUBUNIT ALPHA, ... (9 entities in total)
• 機能のキーワード: hydrolase, urease, sporosarcina pasteurii, nickel, metalloenzyme, 1, 4-benzoquinone
• 由来する生物種: SPOROSARCINA PASTEURII; 詳細
• 細胞内の位置: Cytoplasm : P41022 P41021 P41020
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 88525.94

構造登録者

Mazzei, L.,Cianci, M.,Musiani, F.,Ciurli, S. (登録日: 2016-01-04, 公開日: 2016-03-23, 最終更新日: 2024-01-10)

主引用文献

Mazzei, L.,Cianci, M.,Musiani, F.,Ciurli, S.
Inactivation of Urease by 1,4-Benzoquinone: Chemistry at the Protein Surface.
Dalton Trans, 45:5455-, 2016

PubMed Abstract: The high activity of urease, a Ni(ii) enzyme, has several adverse effects on human health and agriculture, and its modulation needs the use of inhibitors. 1,4-Benzoquinone (BQ) irreversibly inactivates Sporosarcina pasteurii urease (SPU), with first order kinetics for both the inhibitor and the enzyme. This reaction is stoichiometrically quenched in the presence of sulphite. The 2.07 Å crystal structure of SPU bound to BQ shows the presence of a 1,4-hydroquinone moiety covalently bound to the thiol group of αCys322, a key residue found on the mobile flap regulating the substrate access to the active site. The 1.75 Å crystal structure obtained when sulphite is added to a solution of SPU previously incubated with BQ shows the presence of a 2,5-dihydroxy-benzenesulphonate moiety bound to the αCys322 thiol group. These data reveal how the active site cysteine reacts with a prototypical BQ moiety, found in a large number of natural substances potentially suitable to control the urease activity.

PubMed: 26961812
DOI: 10.1039/C6DT00652C

実験手法

X-RAY DIFFRACTION (2.07 Å)