3CTR
Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP
3CTR の概要
| エントリーDOI | 10.2210/pdb3ctr/pdb |
| 分子名称 | Poly(A)-specific ribonuclease PARN, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| 機能のキーワード | parn, protein-rna-complex, m7g-cap, m7gtp, rna recognition motif, rrm, exonuclease, hydrolase, magnesium, metal-binding, nonsense-mediated mrna decay, nuclease, nucleus, phosphoprotein, rna-binding |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Nucleus : O95453 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12360.39 |
| 構造登録者 | Monecke, T.,Schell, S.,Dickmanns, A.,Ficner, R. (登録日: 2008-04-14, 公開日: 2008-07-29, 最終更新日: 2024-02-21) |
| 主引用文献 | Monecke, T.,Schell, S.,Dickmanns, A.,Ficner, R. Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode. J.Mol.Biol., 382:827-834, 2008 Cited by PubMed Abstract: Poly(A)-specific ribonuclease (PARN) is a processive 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. Interestingly, PARN interacts not only with the 3' end of the mRNA but also with its 5' end as PARN contains an RRM domain that specifically binds both the poly(A) tail and the 7-methylguanosine (m(7)G) cap. The interaction of PARN with the 5' cap of mRNAs stimulates the deadenylation activity and enhances the processivity of this reaction. We have determined the crystal structure of the PARN-RRM domain with a bound m(7)G triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap. The structure of the m(7)G binding pocket is located outside of the canonical RNA-binding surface of the RRM domain and differs significantly from that of other m(7)G-cap-binding proteins. The crystal structure also shows a remarkable conformational flexibility of the RRM domain, leading to a perfect exchange of two alpha-helices with an adjacent protein molecule in the crystal lattice. PubMed: 18694759DOI: 10.1016/j.jmb.2008.07.073 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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