3UBP

DIAMIDOPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE

3UBP の概要

• エントリーDOI: 10.2210/pdb3ubp/pdb
• 分子名称: PROTEIN (UREASE GAMMA SUBUNIT), PROTEIN (UREASE BETA SUBUNIT), PROTEIN (UREASE ALPHA SUBUNIT), ... (6 entities in total)
• 機能のキーワード: urease, bacillus pasteurii, nickel, diamidophosphate, metalloenzyme, hydrolase
• 由来する生物種: Sporosarcina pasteurii; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P41022 P41021 P41020
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87022.73

構造登録者

Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Miletti, S.,Mangani, S.,Ciurli, S. (登録日: 1998-12-16, 公開日: 1999-12-17, 最終更新日: 2023-11-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)