6RVZ

Crystal structure of ANGEL2, a 2',3'-cyclic phosphatase, in complex with adenosine-2',3'-vanadate

6RVZ の概要

• エントリーDOI: 10.2210/pdb6rvz/pdb
• 関連するPDBエントリー: 6R6L
• 分子名称: Protein angel homolog 2, adenosine-2',3'-vanadate, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: phosphatase, ccr4d, rna binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49251.13

構造登録者

Kroupova, A.,Jinek, M. (登録日: 2019-06-03, 公開日: 2020-05-20, 最終更新日: 2024-05-01)

主引用文献

Pinto, P.H.,Kroupova, A.,Schleiffer, A.,Mechtler, K.,Jinek, M.,Weitzer, S.,Martinez, J.
ANGEL2 is a member of the CCR4 family of deadenylases with 2',3'-cyclic phosphatase activity.
Science, 369:524-530, 2020

PubMed Abstract: RNA molecules are frequently modified with a terminal 2',3'-cyclic phosphate group as a result of endonuclease cleavage, exonuclease trimming, or de novo synthesis. During pre-transfer RNA (tRNA) and unconventional messenger RNA (mRNA) splicing, 2',3'-cyclic phosphates are substrates of the tRNA ligase complex, and their removal is critical for recycling of tRNAs upon ribosome stalling. We identified the predicted deadenylase angel homolog 2 (ANGEL2) as a human phosphatase that converts 2',3'-cyclic phosphates into 2',3'-OH nucleotides. We analyzed ANGEL2's substrate preference, structure, and reaction mechanism. Perturbing ANGEL2 expression affected the efficiency of pre-tRNA processing, X-box-binding protein 1 () mRNA splicing during the unfolded protein response, and tRNA nucleotidyltransferase 1 (TRNT1)-mediated CCA addition onto tRNAs. Our results indicate that ANGEL2 is involved in RNA pathways that rely on the ligation or hydrolysis of 2',3'-cyclic phosphates.

PubMed: 32732418
DOI: 10.1126/science.aba9763

実験手法

X-RAY DIFFRACTION (2.1 Å)