1bgu: Difference between revisions

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

OverviewOverview

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.

About this StructureAbout this Structure

1BGU is a Single protein structure of sequence from Bacteriophage t4 with as ligand. Active as DNA beta-glucosyltransferase, with EC number 2.4.1.27 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose., Vrielink A, Ruger W, Driessen HP, Freemont PS, EMBO J. 1994 Aug 1;13(15):3413-22. PMID:8062817

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OCA

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 '''CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-BGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with UDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_beta-glucosyltransferase DNA beta-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.27 2.4.1.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BGU OCA].
+BGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=UDP:'>UDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_beta-glucosyltransferase DNA beta-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.27 2.4.1.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGU OCA].
 ==Reference==
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 [[Category: DNA beta-glucosyltransferase]]
 [[Category: Single protein]]
-[[Category: Driessen, H.P.C.]]
+[[Category: Driessen, H P.C.]]
-[[Category: Freemont, P.S.]]
+[[Category: Freemont, P S.]]
 [[Category: Rueger, W.]]
 [[Category: Vrielink, A.]]
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 [[Category: transferase(glucosyltransferase)]]
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