1KWS

CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR

Summary for 1KWS

• Entry DOI: 10.2210/pdb1kws/pdb
• Related: 1FGG
• Descriptor: BETA-1,3-GLUCURONYLTRANSFERASE 3, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID, ... (4 entities in total)
• Functional Keywords: dxd, ntp binding domain, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane ; Single-pass type II membrane protein : O94766
• Total number of polymer chains: 2
• Total formula weight: 59254.57

Authors

Pedersen, L.C.,Darden, T.A.,Negishi, M. (deposition date: 2002-01-30, release date: 2002-06-19, Last modification date: 2023-08-16)

Primary citation

Pedersen, L.C.,Darden, T.A.,Negishi, M.
Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA.
J.Biol.Chem., 277:21869-21873, 2002

PubMed Abstract: 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.

PubMed: 11950836
DOI: 10.1074/jbc.M112343200

Experimental method

X-RAY DIFFRACTION (2.1 Å)