Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.
Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported.
Leiros
Ingar
I
The European Synchrotron Radiation Facility, 38043 Grenoble CEDEX 9, France.
Moe
Elin
E
Smalås
Arne O
AO
McSweeney
Sean
S
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D045647:DNA Glycosylases / Q000737:chemistry*; D034301:Deinococcus / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D051981:Uracil-DNA Glycosidase
D045647:DNA Glycosylases; D051981:Uracil-DNA Glycosidase