5A6T

1.65 A resolution Sulphite inhibited Sporosarcina pasteurii urease

5A6T の概要

• エントリーDOI: 10.2210/pdb5a6t/pdb
• 分子名称: UREASE SUBUNIT GAMMA, UREASE SUBUNIT BETA, UREASE SUBUNIT ALPHA, ... (8 entities in total)
• 機能のキーワード: hydrolase, urease, nickel, metalloenzyme, sulfite
• 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: 87414.07

構造登録者

Mazzei, L.,Cianci, M.,Benini, S.,Bertini, L.,Musiani, F.,Ciurli, S. (登録日: 2015-07-01, 公開日: 2015-12-02, 最終更新日: 2024-01-10)

主引用文献

Mazzei, L.,Cianci, M.,Benini, S.,Bertini, L.,Musiani, F.,Ciurli, S.
Kinetic and Structural Studies Reveal a Unique Binding Mode of Sulfite to the Nickel Center in Urease.
J.Inorg.Biochem., 154:42-, 2015

PubMed Abstract: Urease is the most efficient enzyme known to date, and catalyzes the hydrolysis of urea using two Ni(II) ions in the active site. Urease is a virulence factor in several human pathogens, while causing severe environmental and agronomic problems. Sporosarcina pasteurii urease has been used extensively in the structural characterization of the enzyme. Sodium sulfite has been widely used as a preservative in urease solutions to prevent oxygen-induced oxidation, but its role as an inhibitor has also been suggested. In the present study, isothermal titration microcalorimetry was used to establish sulfite as a competitive inhibitor for S. pasteurii urease, with an inhibition constant of 0.19mM at pH7. The structure of the urease-sulfite complex, determined at 1.65Å resolution, shows the inhibitor bound to the dinuclear Ni(II) center of urease in a tridentate mode involving bonds between the two Ni(II) ions in the active site and all three oxygen atoms of the inhibitor, supporting the observed competitive inhibition kinetics. This coordination mode of sulfite has never been observed, either in proteins or in small molecule complexes, and could inspire synthetic coordination chemists as well as biochemists to develop urease inhibitors based on this chemical moiety.

PubMed: 26580226
DOI: 10.1016/J.JINORGBIO.2015.11.003

実験手法

X-RAY DIFFRACTION (1.65 Å)