Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase

被引:186
作者
Amaya, MF
Watts, AG
Damager, I
Wehenkel, A
Nguyen, T
Buschiazzo, A
Paris, G
Frasch, AC
Withers, SG
Alzari, PM
机构
[1] Inst Pasteur, CNRS, URA 2185, Unite Biochim Struct, F-75724 Paris, France
[2] Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada
[3] Univ Gen San Martin, Inst Invest Biotecnol, RA-1650 San Martin, Argentina
关键词
D O I
10.1016/j.str.2004.02.036
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 traps-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.
引用
收藏
页码:775 / 784
页数:10
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