7Q82

Crystal structure of the methyltransferase-ribozyme 1, Thallium derivative (with 1-methyl-adenosine)

7Q82 の概要

• エントリーDOI: 10.2210/pdb7q82/pdb
• 関連するPDBエントリー: 7Q7X
• 分子名称: RNA 1, RNA 2, RNA 3, ... (6 entities in total)
• 機能のキーワード: mtr1, methyltransferase ribozyme, ribozyme, rna
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 22053.31

構造登録者

Mieczkowski, M.,Hoebartner, C. (登録日: 2021-11-09, 公開日: 2022-03-23, 最終更新日: 2024-01-31)

主引用文献

Scheitl, C.P.M.,Mieczkowski, M.,Schindelin, H.,Hobartner, C.
Structure and mechanism of the methyltransferase ribozyme MTR1.
Nat.Chem.Biol., 18:547-555, 2022

PubMed Abstract: RNA-catalyzed RNA methylation was recently shown to be part of the catalytic repertoire of ribozymes. The methyltransferase ribozyme MTR1 catalyzes the site-specific synthesis of 1-methyladenosine (mA) in RNA, using O-methylguanine (mG) as a methyl group donor. Here, we report the crystal structure of MTR1 at a resolution of 2.8 Å, which reveals a guanine-binding site reminiscent of natural guanine riboswitches. The structure represents the postcatalytic state of a split ribozyme in complex with the mA-containing RNA product and the demethylated cofactor guanine. The structural data suggest the mechanistic involvement of a protonated cytidine in the methyl transfer reaction. A synergistic effect of two 2'-O-methylated ribose residues in the active site results in accelerated methyl group transfer. Supported by these results, it seems plausible that modified nucleotides may have enhanced early RNA catalysis and that metabolite-binding riboswitches may resemble inactivated ribozymes that have lost their catalytic activity during evolution.

PubMed: 35301481
DOI: 10.1038/s41589-022-00976-x

実験手法

X-RAY DIFFRACTION (2.95 Å)