2boo

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Image:2boo.gif

2boo, resolution 1.80Å

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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] with NO3 as [ligand]. Active as [Hydrolase], with EC number [3.2.2.3]. Structure known Active Site: AC1. 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

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