ArticleJournal of structural biology2012
Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus.
Article in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- Structures of Substrate Complexes of Foamy Viral Protease-Reverse Transcriptase.Journal of virology · 2021Article
- Review
- Review
- Retroviral DNA Transposition: Themes and Variations.Microbiology spectrum · 2014Article
- Inhibition of the ANT(2")-Ia resistance enzyme and rescue of aminoglycoside antibiotic activity by synthetic α-hydroxytropolones.Bioorganic & medicinal chemistry letters · 2014Article
- The biology and synthesis of α-hydroxytropolones.MedChemComm · 2014Article
- Evidence from molecular dynamics simulations of conformational preorganization in the ribonuclease H active site.F1000Research · 2014Article
- Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid.Nucleic acids research · 2013Article
- Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.Bioscience reports · 2012Article
- The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.Retrovirology · 2012Article
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Authors and funding
5 authors.
Funding
Abstract
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 likely mode of recognition. The crystal structure of the RNase H domain complexed with β-thujaplicinol clearly showed that coordination by two divalent cations mediates recognition of the inhibitor.
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