title: The trypanosomal trans-sialidase: two catalytic functions associated with one catalytic site.
abstract: The structure of the trypanosomal trans-sialidase reveals a canonical sialidase catalytic site elaborated with a conformational switch that creates an adjacent binding pocket for lactose.
authors.affiliation: Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria, Australia.
authors.forename: Peter M
authors.initials: PM
authors.lastname: Colman
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Smith
mesh_terms: D000818:Animals; D002384:Catalysis; D020134:Catalytic Domain; D006023:Glycoproteins; D007785:Lactose / Q000737:chemistry; D008024:Ligands; D009439:Neuraminidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D006023:Glycoproteins; D008024:Ligands; D010455:Peptides; C069715:trans-sialidase; D009439:Neuraminidase; D007785:Lactose