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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DOI10.2210/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
Pedersen, L.C.,Darden, T.A.,Negishi, M. (登録日: 2002-01-30, 公開日: 2002-06-19, 最終更新日: 2023-08-16)
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: 11950836
DOI: 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)
構造検証レポート
Validation report summary of 1kws
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-02に公開中

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