2AH2

Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid (covalent intermediate)

Replaces:  1S0K

Summary for 2AH2

• Entry DOI: 10.2210/pdb2ah2/pdb
• Related: 2A75 2AGS
• Descriptor: trans-sialidase, CHLORIDE ION, 5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulopyranosonic acid, ... (6 entities in total)
• Functional Keywords: transglycosidase, covalent intermediate, trypanosoma cruzi, sialic acid, hydrolase
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 1
• Total formula weight: 72088.35

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: 2005-07-27, release date: 2005-08-23, Last modification date: 2024-11-13)

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)