2bgu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2bgu.jpg|left|200px]]
{{Seed}}
[[Image:2bgu.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bgu|  PDB=2bgu  |  SCENE=  }}  
{{STRUCTURE_2bgu|  PDB=2bgu  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_8062817}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8062817 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8062817}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Rueger, W.]]
[[Category: Rueger, W.]]
[[Category: Vrielink, A.]]
[[Category: Vrielink, A.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:16:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:47:52 2008''

Revision as of 04:47, 28 July 2008

File:2bgu.png

Template:STRUCTURE 2bgu

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

Template:ABSTRACT PUBMED 8062817

About this Structure

2BGU is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 07:47:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2bgu&oldid=688441"