1S0I

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

Summary for 1S0I

• Entry DOI: 10.2210/pdb1s0i/pdb
• Related: 1S0J 1S0K
• Related PRD ID: PRD_900025
• Descriptor: trans-sialidase, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: transglycosidase, sialyllactose, trypanosoma cruzi, michaelis complex, hydrolase
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 1
• Total formula weight: 71978.80

Authors

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. (deposition date: 2003-12-31, release date: 2004-05-18, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)