1JIX

T4 Phage BGT in Complex with Ca2+

1JIX の概要

• エントリーDOI: 10.2210/pdb1jix/pdb
• 関連するPDBエントリー: 1BGT 1BGU 1C3J 1JIU 1JIV 1QKJ
• 分子名称: DNA BETA-GLUCOSYLTRANSFERASE, CALCIUM ION, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, 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: 41164.12

構造登録者

Morera, S.,Lariviere, L.,Kurzeck, J.,Aschke-Sonnenborn, U.,Freemont, P.S.,Janin, J.,Ruger, W. (登録日: 2001-07-03, 公開日: 2001-08-15, 最終更新日: 2023-08-16)

主引用文献

Morera, S.,Lariviere, L.,Kurzeck, J.,Aschke-Sonnenborn, U.,Freemont, P.S.,Janin, J.,Ruger, W.
High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.
J.Mol.Biol., 311:569-577, 2001

PubMed Abstract: beta-Glucosyltransferase (BGT) is a DNA-modifying enzyme encoded by bacteriophage T4 that transfers glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA. We report six X-ray structures of the substrate-free and the UDP-bound enzyme. Four also contain metal ions which activate the enzyme, including Mg(2+) in forms 1 and 2 and Mn(2+) or Ca(2+). The substrate-free BGT structure differs by a domain movement from one previously determined in another space group. Further domain movements are seen in the complex with UDP and the four UDP-metal complexes. Mg(2+), Mn(2+) and Ca(2+) bind near the beta-phosphate of the nucleotide, but they occupy slightly different positions and have different ligands depending on the metal and the crystal form. Whilst the metal site observed in these complexes with the product UDP is not compatible with a role in activating glucose transfer, it approximates the position of the positive charge in the oxocarbonium ion thought to form on the glucose moiety of the substrate during catalysis.

PubMed: 11493010
DOI: 10.1006/jmbi.2001.4905

実験手法

X-RAY DIFFRACTION (1.65 Å)