2ah2

Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid (covalent intermediate)

spinqualitylabelsall models 2ah2, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ah2 is a 1 chain structure with sequence from Trypanosoma cruzi. This structure supersedes the now removed PDB entry 1s0k. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, FSI, GOL, IPA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q26966_TRYCR Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. See Also Neuraminidase 3D structures

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