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|2ah2, resolution 1.60Å ()|
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Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid (covalent intermediate)
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.
Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase., Amaya MF, Watts AG, Damager I, Wehenkel A, Nguyen T, Buschiazzo A, Paris G, Frasch AC, Withers SG, Alzari PM, Structure. 2004 May;12(5):775-84. PMID:15130470
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Amaya MF, Watts AG, Damager I, Wehenkel A, Nguyen T, Buschiazzo A, Paris G, Frasch AC, Withers SG, Alzari PM. Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Structure. 2004 May;12(5):775-84. PMID:15130470 doi:http://dx.doi.org/10.1016/j.str.2004.02.036
- Demir O, Roitberg AE. Modulation of catalytic function by differential plasticity of the active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase. Biochemistry. 2009 Apr 21;48(15):3398-406. PMID:19216574 doi:10.1021/bi802230y