逆转录酶
过程性
聚合酶
小鼠白血病病毒
DNA聚合酶
生物
分子生物学
逆转录病毒
DNA
牛白血病病毒
底漆(化妆品)
初级
核糖核酸
化学
病毒学
遗传学
病毒
基因
有机化学
作者
Millie M. Georgiadis,Sven M Jessen,Craig M. Ogata,Alice Telesnitsky,Stephen P. Goff,Wayne A. Hendrickson
出处
期刊:Structure
[Elsevier]
日期:1995-09-01
卷期号:3 (9): 879-892
被引量:141
标识
DOI:10.1016/s0969-2126(01)00223-4
摘要
Reverse transcriptase (RT) converts the single-stranded RNA genome of a retrovirus into a double-stranded DNA copy for integration into the host genome. This process requires ribonuclease H as well as RNA- and DNA-directed DNA polymerase activities. Although the overall organization of HIV-1 RT is known from previously reported crystal structures, no structure of a complex including a metal ion, which is essential for its catalytic activity, has been reported.Here we describe the structures at 1.8 Angstrum resolution of a catalytically active fragment of RT from Moloney murine leukemia virus (MMLV) and at 2.6 Angstrum of a complex of this fragment with Mn2+ coordinated in the polymerase active site. On the basis of similarities with HIV-1 RT and rat DNA polymerase beta, we have modeled template/primer and deoxyribonucleoside 5'-triphosphate substrates into the MMLV RT structure.Our model, in the context of the disposition of evolutionarily conserved residues seen here at high resolution, provides new insights into the mechanisms of catalysis, fidelity, processivity and discrimination between deoxyribose and ribose nucleotides.
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