5TD6
C. elegans FOG-3 BTG/Tob domain - H47N, C117A
5TD6 の概要
| エントリーDOI | 10.2210/pdb5td6/pdb |
| 分子名称 | FOG-3 protein, SULFATE ION (3 entities in total) |
| 機能のキーワード | btg/tob, polymer, rna binding, rna binding protein |
| 由来する生物種 | Caenorhabditis elegans |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 32528.72 |
| 構造登録者 | Aoki, S.T.,Bingman, C.A.,Wickens, M.,Kimble, J.E. (登録日: 2016-09-17, 公開日: 2017-09-20, 最終更新日: 2023-10-04) |
| 主引用文献 | Aoki, S.T.,Porter, D.F.,Prasad, A.,Wickens, M.,Bingman, C.A.,Kimble, J. An RNA-Binding Multimer Specifies Nematode Sperm Fate. Cell Rep, 23:3769-3775, 2018 Cited by PubMed Abstract: FOG-3 is a master regulator of sperm fate in Caenorhabditis elegans and homologous to Tob/BTG proteins, which in mammals are monomeric adaptors that recruit enzymes to RNA binding proteins. Here, we determine the FOG-3 crystal structure and in vitro demonstrate that FOG-3 forms dimers that can multimerize. The FOG-3 multimeric structure has a basic surface potential, suggestive of binding nucleic acid. Consistent with that prediction, FOG-3 binds directly to nearly 1,000 RNAs in nematode spermatogenic germ cells. Most binding is to the 3' UTR, and most targets (94%) are oogenic mRNAs, even though assayed in spermatogenic cells. When tethered to a reporter mRNA, FOG-3 represses its expression. Together these findings elucidate the molecular mechanism of sperm fate specification and reveal the evolution of a protein from monomeric to multimeric form with acquisition of a distinct mode of mRNA repression. PubMed: 29949762DOI: 10.1016/j.celrep.2018.05.095 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.034 Å) |
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