4KYS

Clostridium botulinum thiaminase I in complex with thiamin

4KYS の概要

• エントリーDOI: 10.2210/pdb4kys/pdb
• 分子名称: Thiamine pyridinylase I, 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM, CITRIC ACID, ... (5 entities in total)
• 機能のキーワード: periplasmic binding protein type 2 fold, thiaminase i, thiamin degradation, transferase
• 由来する生物種: Clostridium botulinum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99031.76

構造登録者

Sikowitz, M.D.,Shome, B.,Zhang, Y.,Begley, T.P.,Ealick, S.E. (登録日: 2013-05-29, 公開日: 2013-10-30, 最終更新日: 2024-02-28)

主引用文献

Sikowitz, M.D.,Shome, B.,Zhang, Y.,Begley, T.P.,Ealick, S.E.
Structure of a Clostridium botulinum C143S Thiaminase I/Thiamin Complex Reveals Active Site Architecture.
Biochemistry, 52:7830-7839, 2013

PubMed Abstract: Thiaminases are responsible for the degradation of thiamin and its metabolites. Two classes of thiaminases have been identified based on their three-dimensional structures and their requirements for a nucleophilic second substrate. Although the reactions of several thiaminases have been characterized, the physiological role of thiamin degradation is not fully understood. We have determined the three-dimensional X-ray structure of an inactive C143S mutant of Clostridium botulinum (Cb) thiaminase I with bound thiamin at 2.2 Å resolution. The C143S/thiamin complex provides atomic level details of the orientation of thiamin upon binding to Cb-thiaminase I and the identity of active site residues involved in substrate binding and catalysis. The specific roles of active site residues were probed by using site directed mutagenesis and kinetic analyses, leading to a detailed mechanism for Cb-thiaminase I. The structure of Cb-thiaminase I is also compared to the functionally similar but structurally distinct thiaminase II.

PubMed: 24079939
DOI: 10.1021/bi400841g

実験手法

X-RAY DIFFRACTION (2.18 Å)