6RW0
Crystal structure of ANGEL2, a 2',3'-cyclic phosphatase
Summary for 6RW0
| Entry DOI | 10.2210/pdb6rw0/pdb |
| Related | 6RVZ |
| Descriptor | Protein angel homolog 2, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | phosphatase, ccr4d, rna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 48669.70 |
| Authors | Kroupova, A.,Jinek, M. (deposition date: 2019-06-03, release date: 2020-05-20, Last modification date: 2024-01-24) |
| Primary citation | 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 Cited by 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: 32732418DOI: 10.1126/science.aba9763 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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