Nucleic Acids Research, Vol 26, Issue 21 4880-4887, Copyright © 1998 by Oxford University Press
R Ravishankar, M Bidya Sagar, S Roy, K Purnapatre, P Handa, U Varshney and M Vijayan
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.
ARTICLES
X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG
Molecular Biophysics Unit and Department of Microbiology and Cell Biology, Indian Institute of Science,Bangalore 560 012, India.
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