4UBP

STRUCTURE OF BACILLUS PASTEURII UREASE INHIBITED WITH ACETOHYDROXAMIC ACID AT 1.55 A RESOLUTION

4UBP の概要

• エントリーDOI: 10.2210/pdb4ubp/pdb
• 分子名称: PROTEIN (UREASE (CHAIN A)), PROTEIN (UREASE (CHAIN B)), PROTEIN (UREASE (CHAIN C)), ... (6 entities in total)
• 機能のキーワード: urease, bacillus pasteurii, nickel, acetohydroxamic acid, metalloenzyme, hydrolase
• 由来する生物種: Sporosarcina pasteurii; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87001.77

構造登録者

Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Ciurli, S.,Mangani, S. (登録日: 1999-02-25, 公開日: 2000-03-06, 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.
The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution.
J.Biol.Inorg.Chem., 5:110-118, 2000

PubMed Abstract: The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 A resolution, 99.5% completeness, data redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the active site are separated by a distance of 3.53 A. The structure clearly shows the binding mode of the inhibitor anion, symmetrically bridging the two Ni ions in the active site through the hydroxamate oxygen and chelating one Ni ion through the carbonyl oxygen. The flexible flap flanking the active site cavity is in the open conformation. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.

PubMed: 10766443
DOI: 10.1007/s007750050014

実験手法

X-RAY DIFFRACTION (1.55 Å)