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Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
Published on: May 9, 2025
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Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and
Jennifer L Stamos1, Alfred M Lentzsch1, Alan M Lambowitz1
1Institute for Cellular and Molecular Biology and Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
Molecular Cell
|November 21, 2017
Summary
Bacterial group II intron reverse transcriptases (RTs) are key to intron mobility and RNA splicing. Their structure reveals surprising similarities to viral RNA-dependent RNA polymerases, offering insights into RT evolution.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Bacterial group II intron reverse transcriptases (RTs) are crucial for intron mobility and RNA splicing.
- They represent evolutionary precursors to various retroelements and eukaryotic spliceosomal proteins.
Purpose of the Study:
- To determine the crystal structure of a full-length thermostable group II intron RT.
- To elucidate the structural basis for its interaction with RNA-DNA substrates and incoming nucleotides.
Main Methods:
- X-ray crystallography at 3.0-Å resolution.
- Complex formation of the RT with an RNA template-DNA primer duplex and a deoxynucleotide triphosphate (dNTP).
Main Results:
- The structure reveals distinct template-primer binding and active site features compared to retroviral RTs.
- Remarkable similarities were observed between the group II intron RT and viral RNA-dependent RNA polymerases.
- Novel structural features potentially explain the unique biochemical properties of group II intron RTs.
Conclusions:
- The determined structure provides a prototype for related non-LTR retroelement RTs in bacteria and eukaryotes.
- It sheds light on the evolution of protein structural features for reverse transcription and intron splicing.
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