2WGZ
Crystal structure of alpha-1,3 galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNP-beta-Gal)
Summary for 2WGZ
| Entry DOI | 10.2210/pdb2wgz/pdb |
| Related | 1FG5 1G8O 1G93 1GWV 1GWW 1GX0 1GX4 1K4V 1O7O 1O7Q 1VZT 1VZU 1VZX 2JCJ 2JCK 2JCL 2JCO 2VFZ 2VS3 2VS4 2VS5 2VXL 2VXM |
| Descriptor | N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYL TRANSFERASE, 4-nitrophenyl beta-D-galactopyranoside, MANGANESE (II) ION, ... (8 entities in total) |
| Functional Keywords | galactosyltransferase, glycoprotein, metal-binding, signal-anchor, alpha-1, membrane, manganese, transferase, substrate binding, glycosyltransferase, transmembrane, golgi apparatus, enzyme kinetics |
| Biological source | BOS TAURUS (BOVINE) |
| Total number of polymer chains | 2 |
| Total formula weight | 70585.99 |
| Authors | Jamaluddin, H.,Tumbale, P.,Ferns, T.A.,Thiyagarajan, N.,Brew, K.,Acharya, K.R. (deposition date: 2009-04-28, release date: 2009-06-16, Last modification date: 2023-12-13) |
| Primary citation | Jamaluddin, H.,Tumbale, P.,Ferns, T.A.,Thiyagarajan, N.,Brew, K.,Acharya, K.R. Crystal Structure of Alpha-1,3 Galactosyltransferase (Alpha3Gt) in a Complex with P-Nitrophenyl-Beta-Galactoside (Pnpbetagal). Biochem.Biophys.Res.Commun., 385:601-, 2009 Cited by PubMed Abstract: The specificities of glycosyltransferases make them useful for the synthesis of biologically active oligosaccharides, but also restrict their range of products. In substrate engineering, substrate promiscuity is enhanced by attaching removable interactive groups to weak substrates. Thus, the attachment of betap-nitrophenyl converts galactose from a poor into a good substrate of alpha-1,3-galactosyltransferase. The crystallographic structure of a complex of alpha3GT containing p-nitrophenyl-beta-galactoside shows that the p-nitrophenyl binds similarly to the N-acetylglucosamine of the substrate, N-acetyllactosamine, interacting with the indole of Trp249. p-Nitrophenyl, unlike N-acetylglucosamine, makes no H-bonds but has more non-polar interactions, making it an effective monosaccharide mimetic. PubMed: 19486884DOI: 10.1016/J.BBRC.2009.05.111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
Download full validation report
