4AC7

The crystal structure of Sporosarcina pasteurii urease in complex with citrate

4AC7 の概要

• エントリーDOI: 10.2210/pdb4ac7/pdb
• 関連するPDBエントリー: 1IE7 1S3T 1UBP 2UBP 3UBP 4UBP
• 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: hydrolase, bacillus pasteurii
• 由来する生物種: SPOROSARCINA PASTEURII; 詳細
• 細胞内の位置: Cytoplasm : P41022 P41021 P41020
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 88155.72

構造登録者

Benini, S.,Kosikowska, P.,Cianci, M.,Gonzalez Vara, A.,Berlicki, L.,Ciurli, S. (登録日: 2011-12-14, 公開日: 2013-01-16, 最終更新日: 2023-12-20)

主引用文献

Benini, S.,Kosikowska, P.,Cianci, M.,Mazzei, L.,Vara, A.G.,Berlicki, L.,Ciurli, S.
The Crystal Structure of Sporosarcina Pasteurii Urease in a Complex with Citrate Provides New Hints for Inhibitor Design.
J.Biol.Inorg.Chem., 18:391-, 2013

PubMed Abstract: Urease, the enzyme that catalyses the hydrolysis of urea, is a virulence factor for a large number of ureolytic bacterial human pathogens. The increasing resistance of these pathogens to common antibiotics as well as the need to control urease activity to improve the yield of soil nitrogen fertilization in agricultural applications has stimulated the development of novel classes of molecules that target urease as enzyme inhibitors. We report on the crystal structure at 1.50-Å resolution of a complex formed between citrate and urease from Sporosarcina pasteurii, a widespread and highly ureolytic soil bacterium. The fit of the ligand to the active site involves stabilizing interactions, such as a carboxylate group that binds the nickel ions at the active site and several hydrogen bonds with the surrounding residues. The citrate ligand has a significantly extended structure compared with previously reported ligands co-crystallized with urease and thus represents a unique and promising scaffold for the design of new, highly active, stable, selective inhibitors.

PubMed: 23412551
DOI: 10.1007/S00775-013-0983-7

実験手法

X-RAY DIFFRACTION (1.5 Å)