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9ETK

Crystal structure of Vibrio cholerae RNase AM

9ETK の概要
エントリーDOI10.2210/pdb9etk/pdb
分子名称Metal-dependent phosphoesterases (PHP family), GLYCEROL, SULFATE ION, ... (6 entities in total)
機能のキーワードrnase, exoribonuclease, hydrolase
由来する生物種Vibrio cholerae
タンパク質・核酸の鎖数1
化学式量合計33699.99
構造登録者
Lormand, J.D.,Sondermann, H. (登録日: 2024-03-26, 公開日: 2024-09-11, 最終更新日: 2025-03-26)
主引用文献Kim, S.K.,Orr, M.W.,Turdiev, H.,Jenkins, C.C.,Lormand, J.D.,Myers, T.M.,Burnim, A.A.,Carter, J.A.,Kung, W.C.,Jiang, X.,Sondermann, H.,Winkler, W.C.,Lee, V.T.
Diribonuclease activity eliminates toxic diribonucleotide accumulation.
Cell Rep, 43:114759-114759, 2024
Cited by
PubMed Abstract: RNA degradation is a central process required for transcriptional regulation. Eventually, this process degrades diribonucleotides into mononucleotides by specific diribonucleases. In Escherichia coli, oligoribonuclease (Orn) serves this function and is unique as the only essential exoribonuclease. Yet, related organisms, such as Pseudomonas aeruginosa, display a growth defect but are viable without Orn, contesting its essentiality. Here, we take advantage of P. aeruginosa orn mutants to screen for suppressors that restore colony morphology and identified yciV. Purified YciV (RNase AM) exhibits diribonuclease activity. While RNase AM is present in all γ-proteobacteria, phylogenetic analysis reveals differences that map to the active site. RNase AM expression in E. coli eliminates the necessity of orn. Together, these results show that diribonuclease activity prevents toxic diribonucleotide accumulation in γ-proteobacteria, suggesting that diribonucleotides may be utilized to monitor RNA degradation efficacy. Because higher eukaryotes encode Orn, these observations indicate a conserved mechanism for monitoring RNA degradation.
PubMed: 39276351
DOI: 10.1016/j.celrep.2024.114759
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.48 Å)
構造検証レポート
Validation report summary of 9etk
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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