6QDY

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

Summary for 6QDY

• Entry DOI: 10.2210/pdb6qdy/pdb
• Descriptor: Urease subunit gamma, Urease subunit beta, Urease subunit alpha, ... (9 entities in total)
• Functional Keywords: urease, sporosarcina pasteurii, nickel, urea, hydrolase
• Biological source: Sporosarcina pasteurii (Bacillus pasteurii); More
• Total number of polymer chains: 3
• Total formula weight: 87310.92

Authors

Mazzei, L.,Cianci, M.,Benini, S.,Ciurli, S. (deposition date: 2019-01-03, release date: 2019-11-13, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.416 Å)