作者
Dongwen Zhou, Suhman Chung, Maria Miller, Stuart FJ Le Grice, Alexander Wlodawer
发表日期
2012/3/1
期刊
Journal of Structural Biology
卷号
177
期号
3
页码范围
638-645
出版商
Academic Press
简介
The ribonuclease H (RNase H) domain of retroviral reverse transcriptase (RT) plays a critical role in the life cycle by degrading the RNA strands of DNA/RNA hybrids. In addition, RNase H activity is required to precisely remove the RNA primers from nascent (−) and (+) strand DNA. We report here three crystal structures of the RNase H domain of xenotropic murine leukemia virus-related virus (XMRV) RT, namely (i) the previously identified construct from which helix C was deleted, (ii) the intact domain, and (iii) the intact domain complexed with an active site α-hydroxytropolone inhibitor. Enzymatic assays showed that the intact RNase H domain retained catalytic activity, whereas the variant lacking helix C was only marginally active, corroborating the importance of this helix for enzymatic activity. Modeling of the enzyme-substrate complex elucidated the essential role of helix C in binding a DNA/RNA hybrid and its …
学术搜索中的文章
D Zhou, S Chung, M Miller, SFJ Le Grice, A Wlodawer - Journal of Structural Biology, 2012