4OL8

Ty3 reverse transcriptase bound to DNA/RNA

Summary for 4OL8

• Entry DOI: 10.2210/pdb4ol8/pdb
• Descriptor: Reverse transcriptase/ribonuclease H, 5'-R(*CP*UP*GP*AP*GP*AP*GP*AP*GP*AP*GP*GP*AP*AP*GP*AP*UP*G)-3', 5'-D(*CP*AP*TP*CP*TP*TP*CP*CP*TP*CP*TP*CP*TP*CP*TP*C)-3', ... (5 entities in total)
• Functional Keywords: protein-dna/rna, reverse transcription, dna/rna binding, transferase, hydrolase-rna-dna complex, hydrolase/rna/dna
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: Q99315
• Total number of polymer chains: 8
• Total formula weight: 241729.32

Authors

Nowak, E.,Miller, J.T.,Bona, M.K.,Studnicka, J.,Szczepanowski, R.H.,Jurkowski, J.,Le Grice, S.F.J.,Nowotny, M. (deposition date: 2014-01-23, release date: 2014-03-05, Last modification date: 2024-11-20)

Primary citation

Nowak, E.,Miller, J.T.,Bona, M.K.,Studnicka, J.,Szczepanowski, R.H.,Jurkowski, J.,Le Grice, S.F.,Nowotny, M.
Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry.
Nat.Struct.Mol.Biol., 21:389-396, 2014

PubMed Abstract: Retrotransposons are a class of mobile genetic elements that replicate by converting their single-stranded RNA intermediate to double-stranded DNA through the combined DNA polymerase and ribonuclease H (RNase H) activities of the element-encoded reverse transcriptase (RT). Although a wealth of structural information is available for lentiviral and gammaretroviral RTs, equivalent studies on counterpart enzymes of long terminal repeat (LTR)-containing retrotransposons, from which they are evolutionarily derived, is lacking. In this study, we report the first crystal structure of a complex of RT from the Saccharomyces cerevisiae LTR retrotransposon Ty3 in the presence of its polypurine tract-containing RNA-DNA hybrid. In contrast to its retroviral counterparts, Ty3 RT adopts an asymmetric homodimeric architecture whose assembly is substrate dependent. Moreover, our structure and biochemical data suggest that the RNase H and DNA polymerase activities are contributed by individual subunits of the homodimer.

PubMed: 24608367
DOI: 10.1038/nsmb.2785

Experimental method

X-RAY DIFFRACTION (3.1 Å)