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1mz5

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1mz5, resolution 2.20Å ()
Ligands:
Activity: Exo-alpha-sialidase, with EC number 3.2.1.18
Domains: Sialidase
Related: 1mz6, 1mr5, 1ms0, 1ms1, 1ms3, 1ms4, 1ms5, 1ms8, 1ms9
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Trypanosoma rangeli sialidase

Publication Abstract from PubMed

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.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1MZ5 is a 1 chain structure of sequence from Trypanosoma rangeli. Full crystallographic information is available from OCA.

Reference

  • Buschiazzo A, Tavares GA, Campetella O, Spinelli S, Cremona ML, Paris G, Amaya MF, Frasch AC, Alzari PM. Structural basis of sialyltransferase activity in trypanosomal sialidases. EMBO J. 2000 Jan 4;19(1):16-24. PMID:10619840 doi:10.1093/emboj/19.1.16

Page seeded by OCA on Tue Feb 17 16:49:00 2009

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OCA, Fred Vellieux

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