Structural highlights
Function
[UNG_DEIRA] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.,Leiros I, Moe E, Smalas AO, McSweeney S Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:16041069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leiros I, Moe E, Smalas AO, McSweeney S. Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:16041069 doi:10.1107/S090744490501382X
