2WGZ

Crystal structure of alpha-1,3 galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNP-beta-Gal)

2WGZ の概要

• エントリーDOI: 10.2210/pdb2wgz/pdb
• 関連するPDBエントリー: 1FG5 1G8O 1G93 1GWV 1GWW 1GX0 1GX4 1K4V 1O7O 1O7Q 1VZT 1VZU 1VZX 2JCJ 2JCK 2JCL 2JCO 2VFZ 2VS3 2VS4 2VS5 2VXL 2VXM
• 分子名称: N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYL TRANSFERASE, 4-nitrophenyl beta-D-galactopyranoside, MANGANESE (II) ION, ... (8 entities in total)
• 機能のキーワード: galactosyltransferase, glycoprotein, metal-binding, signal-anchor, alpha-1, membrane, manganese, transferase, substrate binding, glycosyltransferase, transmembrane, golgi apparatus, enzyme kinetics
• 由来する生物種: BOS TAURUS (BOVINE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70585.99

構造登録者

Jamaluddin, H.,Tumbale, P.,Ferns, T.A.,Thiyagarajan, N.,Brew, K.,Acharya, K.R. (登録日: 2009-04-28, 公開日: 2009-06-16, 最終更新日: 2023-12-13)

主引用文献

Jamaluddin, H.,Tumbale, P.,Ferns, T.A.,Thiyagarajan, N.,Brew, K.,Acharya, K.R.
Crystal Structure of Alpha-1,3 Galactosyltransferase (Alpha3Gt) in a Complex with P-Nitrophenyl-Beta-Galactoside (Pnpbetagal).
Biochem.Biophys.Res.Commun., 385:601-, 2009

PubMed Abstract: The specificities of glycosyltransferases make them useful for the synthesis of biologically active oligosaccharides, but also restrict their range of products. In substrate engineering, substrate promiscuity is enhanced by attaching removable interactive groups to weak substrates. Thus, the attachment of betap-nitrophenyl converts galactose from a poor into a good substrate of alpha-1,3-galactosyltransferase. The crystallographic structure of a complex of alpha3GT containing p-nitrophenyl-beta-galactoside shows that the p-nitrophenyl binds similarly to the N-acetylglucosamine of the substrate, N-acetyllactosamine, interacting with the indole of Trp249. p-Nitrophenyl, unlike N-acetylglucosamine, makes no H-bonds but has more non-polar interactions, making it an effective monosaccharide mimetic.

PubMed: 19486884
DOI: 10.1016/J.BBRC.2009.05.111

実験手法

X-RAY DIFFRACTION (2.12 Å)