1S0I

Trypanosoma cruzi trans-sialidase in complex with sialyl-lactose (Michaelis complex)

1S0I の概要

• エントリーDOI: 10.2210/pdb1s0i/pdb
• 関連するPDBエントリー: 1S0J 1S0K
• 関連するBIRD辞書のPRD_ID: PRD_900025
• 分子名称: trans-sialidase, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: transglycosidase, sialyllactose, trypanosoma cruzi, michaelis complex, hydrolase
• 由来する生物種: Trypanosoma cruzi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71978.80

構造登録者

Amaya, M.F.,Watts, A.G.,Damager, I.,Wehenkel, A.,Nguyen, T.,Buschiazzo, A.,Paris, G.,Frasch, A.C.,Withers, S.G.,Alzari, P.M. (登録日: 2003-12-31, 公開日: 2004-05-18, 最終更新日: 2024-10-30)

主引用文献

Amaya, M.F.,Watts, A.G.,Damager, I.,Wehenkel, A.,Nguyen, T.,Buschiazzo, A.,Paris, G.,Frasch, A.C.,Withers, S.G.,Alzari, P.M.
Structural Insights into the Catalytic Mechanism of Trypanosoma cruzi trans-Sialidase.
Structure, 12:775-784, 2004

PubMed Abstract: Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the pathogenesis of a number of diseases. However, extensive studies of viral and microbial sialidases have failed to provide a comprehensive picture of their mechanistic properties, in part because the structures of competent enzyme-substrate complexes and reaction intermediates have never been described. Here we report these structures for the Trypanosoma cruzi trans-sialidase (TcTS), showing that catalysis by sialidases occurs via a similar mechanism to that of other retaining glycosidases, but with some intriguing differences that may have evolved in response to the substrate structure.

PubMed: 15130470
DOI: 10.1016/j.str.2004.02.036

実験手法

X-RAY DIFFRACTION (1.6 Å)