1J39

Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate

1J39 の概要

• エントリーDOI: 10.2210/pdb1j39/pdb
• 関連するPDBエントリー: 1C3J 2BGT
• 分子名称: DNA beta-glucosyltransferase, URIDINE-5'-DIPHOSPHATE-GLUCOSE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, gt-b, udp-glucose, transferase
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41562.46

構造登録者

Lariviere, L.,Morera, S. (登録日: 2003-01-21, 公開日: 2003-08-19, 最終更新日: 2023-10-25)

主引用文献

Lariviere, L.,Gueguen-Chaignon, V.,Morera, S.
Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism.
J.Mol.Biol., 330:1077-1086, 2003

PubMed Abstract: T4 phage beta-glucosyltransferase (BGT) is an inverting glycosyltransferase (GT) that transfers glucose from uridine diphospho-glucose (UDP-glucose) to an acceptor modified DNA. BGT belongs to the GT-B structural superfamily, represented, so far, by five different inverting or retaining GT families. Here, we report three high-resolution X-ray structures of BGT and a point mutant solved in the presence of UDP-glucose. The two co-crystal structures of the D100A mutant show that, unlike the wild-type enzyme, this mutation prevents glucose hydrolysis. This strongly indicates that Asp100 is the catalytic base. We obtained the wild-type BGT-UDP-glucose complex by soaking substrate-free BGT crystals. Comparison with a previous structure of BGT solved in the presence of the donor product UDP and an acceptor analogue provides the first model of an inverting GT-B enzyme in which both the donor and acceptor substrates are bound to the active site. The structural analyses support the in-line displacement reaction mechanism previously proposed, locate residues involved in donor substrate specificity and identify the catalytic base.

PubMed: 12860129
DOI: 10.1016/S0022-2836(03)00635-1

実験手法

X-RAY DIFFRACTION (1.87 Å)