6QDY

The crystal structure of Sporosarcina pasteurii urease in complex with its substrate urea

6QDY の概要

• エントリーDOI: 10.2210/pdb6qdy/pdb
• 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: urease, sporosarcina pasteurii, nickel, urea, hydrolase
• 由来する生物種: Sporosarcina pasteurii (Bacillus pasteurii); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87310.92

構造登録者

Mazzei, L.,Cianci, M.,Benini, S.,Ciurli, S. (登録日: 2019-01-03, 公開日: 2019-11-13, 最終更新日: 2024-01-24)

主引用文献

Mazzei, L.,Cianci, M.,Benini, S.,Ciurli, S.
The Structure of the Elusive Urease-Urea Complex Unveils the Mechanism of a Paradigmatic Nickel-Dependent Enzyme.
Angew.Chem.Int.Ed.Engl., 58:7415-7419, 2019

PubMed Abstract: Urease, the most efficient enzyme known, contains an essential dinuclear Ni cluster in the active site. It catalyzes the hydrolysis of urea, inducing a rapid pH increase that has negative effects on human health and agriculture. Thus, the control of urease activity is of utmost importance in medical, pharmaceutical, and agro-environmental applications. All known urease inhibitors are either toxic or inefficient. The development of new and efficient chemicals able to inhibit urease relies on the knowledge of all steps of the catalytic mechanism. The short (microseconds) lifetime of the urease-urea complex has hampered the determination of its structure. The present study uses fluoride to substitute the hydroxide acting as the co-substrate in the reaction, preventing the occurrence of the catalytic steps that follow substrate binding. The 1.42 Å crystal structure of the urease-urea complex, reported here, resolves the enduring debate on the mechanism of this metalloenzyme.

PubMed: 30969470
DOI: 10.1002/anie.201903565

実験手法

X-RAY DIFFRACTION (1.416 Å)