9C6L

Yasminevirus c12orf29, a 5' to 3' RNA ligase

9C6L の概要

• エントリーDOI: 10.2210/pdb9c6l/pdb
• 分子名称: RNA ligase1, ADENOSINE MONOPHOSPHATE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: ligase, atp-grasp, t-rna
• 由来する生物種: Yasminevirus sp. GU-2018
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 186062.86

構造登録者

Hu, Y.,Lopez, V.A.,Tagliabracci, V.S.,Tomchick, D.R. (登録日: 2024-06-07, 公開日: 2024-10-02, 最終更新日: 2025-03-05)

主引用文献

Hu, Y.,Lopez, V.A.,Xu, H.,Pfister, J.P.,Song, B.,Servage, K.A.,Sakurai, M.,Jones, B.T.,Mendell, J.T.,Wang, T.,Wu, J.,Lambowitz, A.M.,Tomchick, D.R.,Pawlowski, K.,Tagliabracci, V.S.
Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.
Proc.Natl.Acad.Sci.USA, 121:e2408249121-e2408249121, 2024

PubMed Abstract: ATP-grasp superfamily enzymes contain a hand-like ATP-binding fold and catalyze a variety of reactions using a similar catalytic mechanism. More than 30 protein families are categorized in this superfamily, and they are involved in a plethora of cellular processes and human diseases. Here, we identify C12orf29 (RLIG1) as an atypical ATP-grasp enzyme that ligates RNA. Human RLIG1 and its homologs autoadenylate on an active site Lys residue as part of a reaction intermediate that specifically ligates RNA halves containing a 5'-phosphate and a 3'-hydroxyl. RLIG1 binds tRNA in cells and can ligate tRNA within the anticodon loop in vitro. Transcriptomic analyses of knockout mice revealed significant alterations in global tRNA levels in the brains of female mice, but not in those of male mice. Furthermore, crystal structures of a RLIG1 homolog from bound to nucleotides revealed a minimal and atypical RNA ligase fold with a conserved active site architecture that participates in catalysis. Collectively, our results identify RLIG1 as an RNA ligase and suggest its involvement in tRNA biology.

PubMed: 39388274
DOI: 10.1073/pnas.2408249121

実験手法

X-RAY DIFFRACTION (2.7 Å)