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9FN2

Crystal structure of the alkyltransferase ribozyme SAMURI co-crystallized with SAM

これはPDB形式変換不可エントリーです。
9FN2 の概要
エントリーDOI10.2210/pdb9fn2/pdb
関連するPDBエントリー9FN3
分子名称SAMURI-SAM, MAGNESIUM ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
機能のキーワードalkylation ribozyme, sam, methylation, samuri, rna
由来する生物種synthetic construct
タンパク質・核酸の鎖数2
化学式量合計38559.29
構造登録者
Chen, H.-A.,Okuda, T.,Lenz, A.-K.,Scheitl, C.P.M.,Schindelin, H.,Hoebartner, C. (登録日: 2024-06-07, 公開日: 2025-01-22, 最終更新日: 2025-02-05)
主引用文献Chen, H.A.,Okuda, T.,Lenz, A.K.,Scheitl, C.P.M.,Schindelin, H.,Hobartner, C.
Structure and catalytic activity of the SAM-utilizing ribozyme SAMURI.
Nat.Chem.Biol., 2025
Cited by
PubMed Abstract: Ribozymes that catalyze site-specific RNA modification have recently gained increasing interest for their ability to mimic methyltransferase enzymes and for their application to install molecular tags. Recently, we reported SAMURI as a site-specific alkyltransferase ribozyme using S-adenosylmethionine (SAM) or a stabilized analog to transfer a methyl or propargyl group to N of an adenosine. Here, we report the crystal structures of SAMURI in the postcatalytic state. The structures reveal a three-helix junction with the catalytic core folded into four stacked layers, harboring the cofactor and the modified nucleotide. Detailed structure-activity analyses explain the cofactor scope and the structural basis for site selectivity. A structural comparison of SAMURI with SAM riboswitches sheds light on how the synthetic ribozyme overcomes the strategies of natural riboswitches to avoid self-methylation. Our results suggest that SAM and its analogs may serve as substrates for various RNA-catalyzed reactions, for which the corresponding ribozymes remain to be identified.
PubMed: 39779902
DOI: 10.1038/s41589-024-01808-w
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 9fn2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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