5nr9

A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (alpha-3GalT) Supports a Conserved Reaction Mechanism for Retaining Glycosyltransferases - Unliganded alpha-3GalT

spinqualitylabelsall models 5nr9, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nr9 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GGTA1_BOVIN Transfer of galactose from UDP-galactose to an acceptor molecule (R). Publication Abstract from PubMed Glycosyltransferases (GTs) are a key family of enzymes that catalyses the synthesis of glycosidic bonds in all living organisms. The reaction involves the transfer of a glycosyl moiety and can proceed with retention or inversion of the anomeric configuration. To date, the elucidation of the catalytic mechanism of retaining GTs is of great controversy, particularly for those enzymes containing a putative nucleophilic residue in the active site, for which a double-displacement mechanism has been suggested. Here, we report native ternary complexes of the retaining alpha1,3-Galactosyltransferase (alpha3GalT) from Bos taurus - containing such a nucleophile in the active site - in a productive mode for catalysis, in the presence of its sugar donor UDP-Gal, the acceptor substrate lactose, and the divalent cation cofactor. This new experimental evidence supports a front-side substrate-assisted SNi-type reaction for alpha3GalT, and suggests a conserved common catalytic mechanism among retaining GTs. Structural Snapshots of the Reaction Center of Family GT6 alpha1,3-Galactosyltransferase with Native Substrates. Insights into the Catalytic Mechanism of Retaining Glycosyltransferases.,Guerin ME, Albesa-Jove D, Sainz-Polo MA, Marina A Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201707922. PMID:28960760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA