3UBP

DIAMIDOPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE

Summary for 3UBP

• Entry DOI: 10.2210/pdb3ubp/pdb
• Descriptor: PROTEIN (UREASE GAMMA SUBUNIT), PROTEIN (UREASE BETA SUBUNIT), PROTEIN (UREASE ALPHA SUBUNIT), ... (6 entities in total)
• Functional Keywords: urease, bacillus pasteurii, nickel, diamidophosphate, metalloenzyme, hydrolase
• Biological source: Sporosarcina pasteurii; More
• Cellular location: Cytoplasm (By similarity): P41022 P41021 P41020
• Total number of polymer chains: 3
• Total formula weight: 87022.73

Authors

Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Miletti, S.,Mangani, S.,Ciurli, S. (deposition date: 1998-12-16, release date: 1999-12-17, Last modification date: 2023-11-15)

Primary citation

Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Miletti, S.,Ciurli, S.,Mangani, S.
A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
Structure Fold.Des., 7:205-216, 1999

PubMed Abstract: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mineralization, using a bimetallic nickel centre. The role of the active site metal ions and amino acid residues has not been elucidated to date. Many pathologies are associated with the activity of ureolytic bacteria, and the efficiency of soil nitrogen fertilization with urea is severely decreased by urease activity. Therefore, the development of urease inhibitors would lead to a reduction of environmental pollution, to enhanced efficiency of nitrogen uptake by plants, and to improved therapeutic strategies for treatment of infections due to ureolytic bacteria. Structure-based design of urease inhibitors would require knowledge of the enzyme mechanism at the molecular level.

PubMed: 10368287
DOI: 10.1016/S0969-2126(99)80026-4

Experimental method

X-RAY DIFFRACTION (2 Å)