3WHS

Crystal structure of Bacillus subtilis gamma-glutamyltranspeptidase in complex with acivicin

3WHS の概要

• エントリーDOI: 10.2210/pdb3whs/pdb
• 関連するPDBエントリー: 3WHQ 3WHR
• 分子名称: Gamma-glutamyltranspeptidase large chain, Gamma-glutamyltranspeptidase small chain, (2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: glutathione hydrolysis, hydrolase, transferase
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66494.67

構造登録者

Wada, K.,Fukuyama, K. (登録日: 2013-08-30, 公開日: 2014-02-19, 最終更新日: 2024-10-30)

主引用文献

Ida, T.,Suzuki, H.,Fukuyama, K.,Hiratake, J.,Wada, K.
Structure of Bacillus subtilis gamma-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue.
Acta Crystallogr.,Sect.D, 70:607-614, 2014

PubMed Abstract: γ-Glutamyltranspeptidase (GGT) is an enzyme that plays a central role in glutathione metabolism, and acivicin is a classical inhibitor of GGT. Here, the structure of acivicin bound to Bacillus subtilis GGT determined by X-ray crystallography to 1.8 Å resolution is presented, in which it binds to the active site in a similar manner to that in Helicobacter pylori GGT, but in a different binding mode to that in Escherichia coli GGT. In B. subtilis GGT, acivicin is bound covalently through its C3 atom with sp2 hybridization to Thr403 Oγ, the catalytic nucleophile of the enzyme. The results show that acivicin-binding sites are common, but the binding manners and orientations of its five-membered dihydroisoxazole ring are diverse in the binding pockets of GGTs.

PubMed: 24531494
DOI: 10.1107/S1399004713031222

実験手法

X-RAY DIFFRACTION (1.8 Å)