1eui: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1eui.gif|left|200px]]
{{Seed}}
[[Image:1eui.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eui|  PDB=1eui  |  SCENE=  }}  
{{STRUCTURE_1eui|  PDB=1eui  |  SCENE=  }}  


'''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN'''
===ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN===




==Overview==
<!--
Uracil-DNA glycosylase (UDG), a key highly conserved DNA repair enzyme involved in uracil excision repair, was discovered in Escherichia coli . The Bacillus subtilis bacteriophage, PBS-1 and PBS-2, which contain dUMP residues in their DNA, express a UDG inhibitor protein, Ugi which binds to UDG very tightly to form a physiologically irreversible complex. The X-ray analysis of the E. coli UDG ( Ec UDG)-Ugi complex at 3.2 A resolution, leads to the first structure elucidation of a bacterial UDG molecule. This structure is similar to the enzymes from human and viral sources. A comparison of the available structures involving UDG permits the delineation of the constant and the variable regions of the molecule. Structural comparison and mutational analysis also indicate that the mode of action of the enzyme from these sources are the same. The crystal structure shows a remarkable spatial conservation of the active site residues involved in DNA binding in spite of significant differences in the structure of the enzyme-inhibitor complex, in comparison with those from the mammalian and viral sources. Ec UDG could serve as a prototype for UDGs from pathogenic prokaryotes, and provide a framework for possible drug development against such pathogens with emphasis on features of the molecule that differ from those in the human enzyme.
The line below this paragraph, {{ABSTRACT_PUBMED_9776748}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9776748 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9776748}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Glycosylase]]
[[Category: Glycosylase]]
[[Category: Inhibitor]]
[[Category: Inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:31:53 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:00:33 2008''

Revision as of 23:00, 30 June 2008

File:1eui.png

Template:STRUCTURE 1eui

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

Template:ABSTRACT PUBMED 9776748

About this Structure

1EUI is a Protein complex structure of sequences from Bacillus phage pbs2 and Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG., Ravishankar R, Bidya Sagar M, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M, Nucleic Acids Res. 1998 Nov 1;26(21):4880-7. PMID:9776748

Page seeded by OCA on Tue Jul 1 02:00:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1eui&oldid=594120"