1KWS
CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR
1KWS の概要
エントリーDOI | 10.2210/pdb1kws/pdb |
関連するPDBエントリー | 1FGG |
分子名称 | BETA-1,3-GLUCURONYLTRANSFERASE 3, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID, ... (4 entities in total) |
機能のキーワード | dxd, ntp binding domain, transferase |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Golgi apparatus membrane ; Single-pass type II membrane protein : O94766 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 59254.57 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 11950836DOI: 10.1074/jbc.M112343200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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