1MS1

Monoclinic form of Trypanosoma cruzi trans-sialidase, in complex with 3-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA)

1MS1 の概要

• エントリーDOI: 10.2210/pdb1ms1/pdb
• 関連するPDBエントリー: 1MR5 1MS0 1MS3 1MS4 1MS5 1MS8 1MS9 1MZ5 1MZ6
• 分子名称: trans-sialidase, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: transglycosylation, beta-propeller, protein-carbohydrate interactions, sialidase, hydrolase
• 由来する生物種: Trypanosoma cruzi
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 143637.31

構造登録者

Buschiazzo, A.,Amaya, M.F.,Cremona, M.L.,Frasch, A.C.,Alzari, P.M. (登録日: 2002-09-19, 公開日: 2003-03-25, 最終更新日: 2024-12-25)

主引用文献

Buschiazzo, A.,Amaya, M.F.,Cremona, M.L.,Frasch, A.C.,Alzari, P.M.
The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis
Mol.Cell, 10:757-768, 2002

PubMed Abstract: Trans-sialidases (TS) are GPI-anchored surface enzymes expressed in specific developmental stages of trypanosome parasites like Trypanosoma cruzi, the etiologic agent of Chagas disease, and T. brucei, the causative agent of sleeping sickness. TS catalyzes the transfer of sialic acid residues from host to parasite glycoconjugates through a transglycosidase reaction that appears to be critical for T. cruzi survival and cell invasion capability. We report here the structure of the T. cruzi trans-sialidase, alone and in complex with sugar ligands. Sialic acid binding is shown to trigger a conformational switch that modulates the affinity for the acceptor substrate and concomitantly creates the conditions for efficient transglycosylation. The structure provides a framework for the structure-based design of novel inhibitors with potential therapeutic applications.

PubMed: 12419220
DOI: 10.1016/S1097-2765(02)00680-9

実験手法

X-RAY DIFFRACTION (1.8 Å)