2BGT

CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE

Summary for 2BGT

• Entry DOI: 10.2210/pdb2bgt/pdb
• Descriptor: BETA-GLUCOSYLTRANSFERASE (2 entities in total)
• Functional Keywords: transferase (glycosyltransferase)
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 40719.88

Authors

Vrielink, A.,Rueger, W.,Driessen, H.P.C.,Freemont, P.S. (deposition date: 1994-06-09, release date: 1995-12-09, Last modification date: 2024-02-14)

Primary citation

Vrielink, A.,Ruger, W.,Driessen, H.P.,Freemont, P.S.
Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose.
EMBO J., 13:3413-3422, 1994

PubMed Abstract: Bacteriophage T4 beta-glucosyltransferase (EC 2.4.1.27) catalyses the transfer of glucose from uridine diphosphoglucose to hydroxymethyl groups of modified cytosine bases in T4 duplex DNA forming beta-glycosidic linkages. The enzyme forms part of a phage DNA protection system. We have solved and refined the crystal structure of recombinant beta-glucosyltransferase to 2.2 A resolution in the presence and absence of the substrate, uridine diphosphoglucose. The structure comprises two domains of similar topology, each reminiscent of a nucleotide binding fold. The two domains are separated by a central cleft which generates a concave surface along one side of the molecule. The substrate-bound complex reveals only clear electron density for the uridine diphosphate portion of the substrate. The UDPG is bound in a pocket at the bottom of the cleft between the two domains and makes extensive hydrogen bonding contacts with residues of the C-terminal domain only. The domains undergo a rigid body conformational change causing the structure to adopt a more closed conformation upon ligand binding. The movement of the domains is facilitated by a hinge region between residues 166 and 172. Electrostatic surface potential calculations reveal a large positive potential along the concave surface of the structure, suggesting a possible site for duplex DNA interaction.

PubMed: 8062817

Experimental method

X-RAY DIFFRACTION (2.2 Å)