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1MZ5

Trypanosoma rangeli sialidase

Summary for 1MZ5
Entry DOI10.2210/pdb1mz5/pdb
Related1MR5 1MS0 1MS1 1MS3 1MS4 1MS5 1MS8 1MS9 1MZ6
Descriptorsialidase, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsinibitor complex, trypanosomal sialidase, sialyltransferase, hydrolase
Biological sourceTrypanosoma rangeli
Total number of polymer chains1
Total formula weight70811.49
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 citationBuschiazzo, 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: 10619840
DOI: 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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