1ZIZ

Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Galactose

1ZIZ の概要

• エントリーDOI: 10.2210/pdb1ziz/pdb
• 関連するPDBエントリー: 1ZHJ 1ZI1 1ZI3 1ZI4 1ZI5 1ZJ0 1ZJ1 1ZJ2 1ZJ3 1ZJO 1ZJP
• 分子名称: ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase), beta-D-galactopyranose, MERCURY (II) ION, ... (5 entities in total)
• 機能のキーワード: gtb, abo(h), h-antigen, blood group, transferase, retaining
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein: P16442
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35575.59

構造登録者

Letts, J.A.,Rose, N.L.,Fang, Y.R.,Barry, C.H.,Borisova, S.N.,Seto, N.O.,Palcic, M.M.,Evans, S.V. (登録日: 2005-04-27, 公開日: 2005-12-13, 最終更新日: 2023-08-23)

主引用文献

Letts, J.A.,Rose, N.L.,Fang, Y.R.,Barry, C.H.,Borisova, S.N.,Seto, N.O.,Palcic, M.M.,Evans, S.V.
Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases.
J.Biol.Chem., 281:3625-3632, 2006

PubMed Abstract: The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.

PubMed: 16326711
DOI: 10.1074/jbc.M507620200

実験手法

X-RAY DIFFRACTION (1.49 Å)