6AR5

Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications (Duplex Only)

6AR5 の概要

• エントリーDOI: 10.2210/pdb6ar5/pdb
• 関連するPDBエントリー: 6AR1 6AR3
• 分子名称: DNA, RNA (3 entities in total)
• 機能のキーワード: duplex, dna-rna complex, dna/rna
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8416.26

構造登録者

Stamos, J.L.,Lentzsch, A.M.,Lambowitz, A.M. (登録日: 2017-08-21, 公開日: 2017-11-29, 最終更新日: 2024-03-13)

主引用文献

Stamos, J.L.,Lentzsch, A.M.,Lambowitz, A.M.
Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications.
Mol. Cell, 68:926-939.e4, 2017

PubMed Abstract: Bacterial group II intron reverse transcriptases (RTs) function in both intron mobility and RNA splicing and are evolutionary predecessors of retrotransposon, telomerase, and retroviral RTs as well as the spliceosomal protein Prp8 in eukaryotes. Here we determined a crystal structure of a full-length thermostable group II intron RT in complex with an RNA template-DNA primer duplex and incoming deoxynucleotide triphosphate (dNTP) at 3.0-Å resolution. We find that the binding of template-primer and key aspects of the RT active site are surprisingly different from retroviral RTs but remarkably similar to viral RNA-dependent RNA polymerases. The structure reveals a host of features not seen previously in RTs that may contribute to distinctive biochemical properties of group II intron RTs, and it provides a prototype for many related bacterial and eukaryotic non-LTR retroelement RTs. It also reveals how protein structural features used for reverse transcription evolved to promote the splicing of both group II and spliceosomal introns.

PubMed: 29153391
DOI: 10.1016/j.molcel.2017.10.024

実験手法

X-RAY DIFFRACTION (2.413 Å)