6rw0 | pdb_00006rw0

Crystal structure of ANGEL2, a 2',3'-cyclic phosphatase

spinqualitylabelsall models 6rw0, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rw0 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: GOL, K, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ANGE2_HUMAN Publication Abstract from PubMed 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 (XBP1) 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. ANGEL2 is a member of the CCR4 family of deadenylases with 2',3'-cyclic phosphatase activity.,Pinto PH, Kroupova A, Schleiffer A, Mechtler K, Jinek M, Weitzer S, Martinez J Science. 2020 Jul 31;369(6503):524-530. doi: 10.1126/science.aba9763. PMID:32732418 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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