1kws
From Proteopedia
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CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR
Overview
Beta1,3-glucuronyltransferase (GlcAT-I) is an essential enzyme involved in, heparan sulfate and chondroitin sulfate biosynthesis. GlcAT-I is an, inverting glycosyltransferase that catalyzes the transfer of glucuronic, acid (GlcUA) to the common growing linker region Galbeta1-3Galbeta1-4Xyl, that is attached to a serine side chain of a core protein. Previously the, structure of GlcAT-I has been solved in the presence of the donor product, UDP and an acceptor analog Galbeta1-3Galbeta1-4Xyl (Pedersen, L. C., Tsuchida, K., Kitagawa, H., Sugahara, K., Darden, T. A. & Negishi, M., (2000) J. Biol. Chem. 275, 34580-34585). Here we report the x-ray crystal, structure of GlcAT-I in complex with the complete donor UDP-GlcUA, thereby, providing structures of an inverting glycosyltransferase in which both the, complete donor and acceptor substrates are present in the active site., This structure supports the in-line displacement reaction mechanism, previously proposed. It also provides information on the essential amino, acid residues that determine donor substrate specificity.
About this Structure
1KWS is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA., Pedersen LC, Darden TA, Negishi M, J Biol Chem. 2002 Jun 14;277(24):21869-73. Epub 2002 Apr 11. PMID:11950836
Page seeded by OCA on Fri Feb 15 16:15:35 2008
Categories: Homo sapiens | Single protein | Darden, T.A. | Negishi, M. | Pedersen, L.C. | MN | UGA | Dxd | Ntp binding domain
