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PDBsum entry 2bgu
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Transferase (glycosyltransferase)
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PDB id
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2bgu
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the DNA modifying enzyme beta-Glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose.
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Authors
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A.Vrielink,
W.Rüger,
H.P.Driessen,
P.S.Freemont.
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Ref.
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Embo J, 1994,
13,
3413-3422.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray studies of t4 phage beta-Glucosyltransferase.
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Authors
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P.S.Freemont,
W.Rüger.
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Ref.
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J Mol Biol, 1988,
203,
525-526.
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PubMed id
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Secondary reference #2
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Title
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T4-Induced alpha- And beta-Glucosyltransferase: cloning of the genes and a comparison of their products based on sequencing data.
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Authors
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J.Tomaschewski,
H.Gram,
J.W.Crabb,
W.Rüger.
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Ref.
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Nucleic Acids Res, 1985,
13,
7551-7568.
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PubMed id
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