期刊
STRUCTURE
卷 24, 期 11, 页码 1960-1971出版社
CELL PRESS
DOI: 10.1016/j.str.2016.09.005
关键词
-
资金
- Platform for Drug Design, Informatics, and Structural Lifescience (PDIS) from the AMED [16am0101042j0005]
- MEXT [25280109, 26242075]
- Institute for Fermentation, Osaka (IFO), Japan
- Grants-in-Aid for Scientific Research [25280109, 16H01410, 26242075] Funding Source: KAKEN
Archaeal NucS nuclease was thought to degrade the single-stranded region of branched DNA, which contains flapped and splayed DNA. However, recent findings indicated that EndoMS, the orthologous enzyme of NucS, specifically cleaves double-stranded DNA (dsDNA) containing mismatched bases. In this study, we determined the structure of the EndoMS-DNA complex. The complex structure of the EndoMS dimer with dsDNA unexpectedly revealed that the mismatched bases were flipped out into binding sites, and the overall architecture most resembled that of restriction enzymes. The structure of the apo form was similar to the reported structure of Pyrococcus abyssi NucS, indicating that movement of the C-terminal domain from the resting state was required for activity. In addition, a model of the EndoMS-PCNA-DNA complex was preliminarily verified with electron microscopy. The structures strongly support the idea that EndoMS acts in a mismatch repair pathway.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据