Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans

被引：26
|
作者：
Leiros, I
Moe, E
Smalås, AO
McSweeney, S
机构：
[1] European Synchrotron Radiat Facil, F-38043 Grenoble, France
[2] Univ Tromso, Norwegian Struct Biol Ctr, N-9037 Tromso, Norway
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷
关键词：
D O I：
10.1107/S090744490501382X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1049 / 1056
页数：8
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