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3I2S

Crystal structure of the hairpin ribozyme with a 2'OMe substrate and N1-deazaadenosine at position A10

3I2S の概要
エントリーDOI10.2210/pdb3i2s/pdb
関連するPDBエントリー3I2P 3I2Q 3I2R 3I2U
分子名称5'-R(*UP*CP*CP*CP*(A2M)P*GP*UP*CP*CP*AP*CP*CP*GP*U)-3', DNA/RNA (30-MER), 5'-R(*UP*CP*GP*UP*GP*GP*UP*AP*CP*AP*UP*UP*AP*CP*CP*UP*GP*CP*C)-3', ... (5 entities in total)
機能のキーワードhairpin ribozyme, n1-deazaadenosine, rna
タンパク質・核酸の鎖数3
化学式量合計20544.53
構造登録者
Wedekind, J.E.,Spitale, R.C.,Krucinska, J. (登録日: 2009-06-29, 公開日: 2009-11-03, 最終更新日: 2023-09-06)
主引用文献Spitale, R.C.,Volpini, R.,Mungillo, M.V.,Krucinska, J.,Cristalli, G.,Wedekind, J.E.
Single-atom imino substitutions at A9 and A10 reveal distinct effects on the fold and function of the hairpin ribozyme catalytic core.
Biochemistry, 48:7777-7779, 2009
Cited by
PubMed Abstract: The hairpin ribozyme cleaves a phosphodiester bond within a cognate substrate. Structural and biochemical data indicate the conserved A9 and A10 bases reside close to the scissile bond but make distinct contributions to catalysis. To investigate these residues, we replaced the imino moiety of each base with N1-deazaadenosine. This single-atom change resulted in an 8-fold loss in k(obs) for A9 and displacement of the base from the active site; no effects were observed for A10. We propose that the imino moiety of A9 promotes a key water-mediated contact that favors transition-state formation, which suggests an enhanced chemical repertoire for RNA.
PubMed: 19634899
DOI: 10.1021/bi9011622
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.75 Å)
構造検証レポート
Validation report summary of 3i2s
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2024-10-30に公開中

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