1MZ5
Trypanosoma rangeli sialidase
Summary for 1MZ5
Entry DOI | 10.2210/pdb1mz5/pdb |
Related | 1MR5 1MS0 1MS1 1MS3 1MS4 1MS5 1MS8 1MS9 1MZ6 |
Descriptor | sialidase, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | inibitor complex, trypanosomal sialidase, sialyltransferase, hydrolase |
Biological source | Trypanosoma rangeli |
Total number of polymer chains | 1 |
Total formula weight | 70811.49 |
Authors | Buschiazzo, A.,Tavares, G.A.,Campetella, O.,Spinelli, S.,Cremona, M.L.,Paris, G.,Amaya, M.F.,Frasch, A.C.C.,Alzari, P.M. (deposition date: 2002-10-05, release date: 2002-10-16, Last modification date: 2024-10-30) |
Primary citation | Buschiazzo, A.,Tavares, G.A.,Campetella, O.,Spinelli, S.,Cremona, M.L.,Paris, G.,Amaya, M.F.,Frasch, A.C.C.,Alzari, P.M. Structural basis of sialyltransferase activity in trypanosomal sialidases Embo J., 19:16-24, 2000 Cited by PubMed Abstract: The intracellular parasite Trypanosoma cruzi, the etiological agent of Chagas disease, sheds a developmentally regulated surface trans-sialidase, which is involved in key aspects of parasite-host cell interactions. Although it shares a common active site architecture with bacterial neuraminidases, the T.cruzi enzyme behaves as a highly efficient sialyltransferase. Here we report the crystal structure of the closely related Trypanosoma rangeli sialidase and its complex with inhibitor. The enzyme folds into two distinct domains: a catalytic beta-propeller fold tightly associated with a lectin-like domain. Comparison with the modeled structure of T.cruzi trans-sialidase and mutagenesis experiments allowed the identification of amino acid substitutions within the active site cleft that modulate sialyltransferase activity and suggest the presence of a distinct binding site for the acceptor carbohydrate. The structures of the Trypanosoma enzymes illustrate how a glycosidase scaffold can achieve efficient glycosyltransferase activity and provide a framework for structure-based drug design. PubMed: 10619840DOI: 10.1093/emboj/19.1.16 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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