|Title||Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase|
|Publication Type||Journal Article|
|Year of Publication||2004|
|Authors||Amaya, MF, Watts, AG, Damager, I, Wehenkel, A, Nguyen, T, Buschiazzo, A, Paris, G, Frasch, AC, Withers, SG, Alzari, PM|
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.