Structural Insights into the Catalytic Mechanism of Trypanosoma cruzi trans-Sialidase
| Autor: | Alejandro Buschiazzo, Maria Fernanda Amaya, Andrew G. Watts, T. Nguyen, Alberto C.C. Frasch, Stephen G. Withers, Gastón Paris, Pedro M. Alzari, Annemarie Wehenkel, Iben Damager |
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| Přispěvatelé: | Biochimie Structurale, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], University of British Columbia (UBC), Universidad Nacional de San Martin (UNSAM), This work was supported by grants from the Human Frontier Science Program Organization, the Institut Pasteur (France), and the CONICET (Argentina). A.C.F. was supported by an International Research Scholar Grant from the Howard Hughes Medical Institute., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2004 |
| Předmět: |
Trypanosoma cruzi
Static Electricity MESH: Glycoproteins Neuraminidase MESH: Catalytic Domain Virulence Crystallography X-Ray 010402 general chemistry Sialidase 01 natural sciences Catalysis Trans-sialidase MESH: Protein Structure Tertiary 03 medical and health sciences Structural Biology Catalytic Domain Hydrolase [CHIM.CRIS]Chemical Sciences/Cristallography Animals MESH: Animals [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Molecular Biology MESH: Static Electricity Glycoproteins 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology MESH: Neuraminidase SUPERFAMILY MESH: Crystallography X-Ray biology.organism_classification Protein Structure Tertiary 0104 chemical sciences Enzyme chemistry Biochemistry MESH: Trypanosoma cruzi |
| Zdroj: | Structure Structure, Elsevier (Cell Press), 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩ Structure, 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩ |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2004.02.036 |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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