2boo
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Sites: | |||||||
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| Activity: | Uridine nucleosidase, with EC number 3.2.2.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.
Overview
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.
About this Structure
2BOO is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:04:41 2008
