2I8E
Structure of SSO1404, a predicted DNA repair-associated protein from Sulfolobus solfataricus P2
2I8E の概要
| エントリーDOI | 10.2210/pdb2i8e/pdb |
| 分子名称 | Hypothetical protein, IODIDE ION (3 entities in total) |
| 機能のキーワード | dna repair, unknown function, structural genomics, midwest center for structural genomics, mcsg, psi, protein structure initiative |
| 由来する生物種 | Sulfolobus solfataricus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12601.08 |
| 構造登録者 | Wang, S.,Zimmerman, M.D.,Kudritska, M.,Chruszcz, M.,Savchenko, A.,Edwards, A.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (登録日: 2006-09-01, 公開日: 2006-09-26, 最終更新日: 2024-11-20) |
| 主引用文献 | Beloglazova, N.,Brown, G.,Zimmerman, M.D.,Proudfoot, M.,Makarova, K.S.,Kudritska, M.,Kochinyan, S.,Wang, S.,Chruszcz, M.,Minor, W.,Koonin, E.V.,Edwards, A.M.,Savchenko, A.,Yakunin, A.F. A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats. J.Biol.Chem., 283:20361-20371, 2008 Cited by PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPRs) together with the associated CAS proteins protect microbial cells from invasion by foreign genetic elements using presently unknown molecular mechanisms. All CRISPR systems contain proteins of the CAS2 family, suggesting that these uncharacterized proteins play a central role in this process. Here we show that the CAS2 proteins represent a novel family of endoribonucleases. Six purified CAS2 proteins from diverse organisms cleaved single-stranded RNAs preferentially within U-rich regions. A representative CAS2 enzyme, SSO1404 from Sulfolobus solfataricus, cleaved the phosphodiester linkage on the 3'-side and generated 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The crystal structure of SSO1404 was solved at 1.6A resolution revealing the first ribonuclease with a ferredoxin-like fold. Mutagenesis of SSO1404 identified six residues (Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37) that are important for enzymatic activity and suggested that Asp-10 might be the principal catalytic residue. Thus, CAS2 proteins are sequence-specific endoribonucleases, and we propose that their role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs. PubMed: 18482976DOI: 10.1074/jbc.M803225200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.59 Å) |
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