1JG7

T4 phage BGT in complex with UDP and Mn2+

Summary for 1JG7

• Entry DOI: 10.2210/pdb1jg7/pdb
• Related: 1BGT 1BGU 1C3J 1JEJ 1JG6 1QKJ
• Descriptor: DNA BETA-GLUCOSYLTRANSFERASE, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, transferase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 41178.98

Authors

Morera, S.,Lariviere, L.,Kurzeck, J.,Aschke-Sonnenborn, U.,Freemont, P.S.,Janin, J.,Ruger, W. (deposition date: 2001-06-23, release date: 2001-08-15, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)