4EYT
Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65
4EYT の概要
| エントリーDOI | 10.2210/pdb4eyt/pdb |
| 関連するPDBエントリー | 4ERD |
| 分子名称 | Telomerase associated protein p65, SULFATE ION (3 entities in total) |
| 機能のキーワード | rna, la protein, larp7, rrm, xrrm, rna binding protein |
| 由来する生物種 | Tetrahymena thermophila 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 93966.18 |
| 構造登録者 | Singh, M.,Wang, Z.,Koo, B.-K.,Patel, A.,Cascio, D.,Collins, K.,Feigon, J. (登録日: 2012-05-01, 公開日: 2012-06-20, 最終更新日: 2023-09-13) |
| 主引用文献 | Singh, M.,Wang, Z.,Koo, B.K.,Patel, A.,Cascio, D.,Collins, K.,Feigon, J. Structural Basis for Telomerase RNA Recognition and RNP Assembly by the Holoenzyme La Family Protein p65. Mol.Cell, 47:16-26, 2012 Cited by PubMed Abstract: Telomerase is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. The catalytic core of Tetrahymena telomerase comprises a ternary complex of telomerase RNA (TER), telomerase reverse transcriptase (TERT), and the essential La family protein p65. NMR and crystal structures of p65 C-terminal domain and its complex with stem IV of TER reveal that RNA recognition is achieved by a combination of single- and double-stranded RNA binding, which induces a 105° bend in TER. The domain is a cryptic, atypical RNA recognition motif with a disordered C-terminal extension that forms an α helix in the complex necessary for hierarchical assembly of TERT with p65-TER. This work provides the first structural insight into biogenesis and assembly of TER with a telomerase-specific protein. Additionally, our studies define a structurally homologous domain (xRRM) in genuine La and LARP7 proteins and suggest a general mode of RNA binding for biogenesis of their diverse RNA targets. PubMed: 22705372DOI: 10.1016/j.molcel.2012.05.018 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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