1LZJ

Glycosyltransferase B + UDP + H antigen acceptor

1LZJ の概要

• エントリーDOI: 10.2210/pdb1lzj/pdb
• 関連するPDBエントリー: 1LZ0 1LZ7 1LZI
• 分子名称: Glycosyltransferase B, alpha-L-fucopyranose-(1-2)-hexyl beta-D-galactopyranoside, MERCURY (II) ION, ... (6 entities in total)
• 機能のキーワード: glycoprotein, transmembrane, signal-anchor, blood group antigen, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35681.19

構造登録者

Patenaude, S.I.,Seto, N.O.L.,Borisova, S.N.,Szpacenko, A.,Marcus, S.L.,Palcic, M.M.,Evans, S.V. (登録日: 2002-06-10, 公開日: 2002-08-28, 最終更新日: 2024-05-22)

主引用文献

Patenaude, S.I.,Seto, N.O.,Borisova, S.N.,Szpacenko, A.,Marcus, S.L.,Palcic, M.M.,Evans, S.V.
The structural basis for specificity in human ABO(H) blood group biosynthesis.
Nat.Struct.Biol., 9:685-690, 2002

PubMed Abstract: The human ABO(H) blood group antigens are produced by specific glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA) uses a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase (GTB) uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. GTA and GTB differ only in the identity of four critical amino acid residues. Crystal structures at 1.8-1.32 A resolution of the GTA and GTB enzymes both free and in complex with disaccharide H-antigen acceptor and UDP reveal the basis for donor and acceptor specificity and show that only two of the critical amino acid residues are positioned to contact donor or acceptor substrates. Given the need for stringent stereo- and regioselectivity in this biosynthesis, these structures further demonstrate that the ability of the two enzymes to distinguish between the A and B donors is largely determined by a single amino acid residue.

PubMed: 12198488
DOI: 10.1038/nsb832

実験手法

X-RAY DIFFRACTION (1.32 Å)