5EIP
apo-structure of YTH domain of SpMmi1
5EIP の概要
| エントリーDOI | 10.2210/pdb5eip/pdb |
| 関連するPDBエントリー | 5EIM |
| 分子名称 | YTH domain-containing protein mmi1 (2 entities in total) |
| 機能のキーワード | yth, mmi1, dsr, rna binding protein |
| 由来する生物種 | Schizosaccharomyces pombe 972h- (Fission yeast) |
| 細胞内の位置 | Nucleus : O74958 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 30420.38 |
| 構造登録者 | |
| 主引用文献 | Wu, B.X.,Xu, J.H.,Su, S.C.,Liu, H.,Gan, J.,Ma, J.B. Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1 Biochem. Biophys. Res. Commun., 491:310-316, 2017 Cited by PubMed Abstract: Meiosis is one of the most dramatic differentiation programs accompanied by a striking change in gene expression profiles in fission yeast Schizosaccharomyces pombe. Whereas a number of meiosis-specific transcripts are expressed untimely in mitotic cells, and the entry of meiosis will be blocked as the accumulation of meiosis-specific mRNAs in the mitotic cells. A YTH domain containing protein Mmi1 was identified as a pivotal effector in a post-transcriptional event termed selective elimination of meiosis-specific mRNAs. Mmi1 can recognize and bind a class of meiosis-specific transcripts expressed inappropriately in mitotic cells, which all contain a conservative region called DSR, as a mark to remove them in cooperation with nuclear exosomes. Here we report the 1.6 Å resolution crystal structure of the Mmi1-YTH domain in complex with a high consensus hexanucleotide motif, which is multiple copied in the DSR region. Our structure observations, supported by site-directed mutations of key residues illustrate the mechanism for specific recognition of DSR-RNA by Mmi1. Moreover, different from other YTH domain family proteins, Mmi1-YTH domain has a distinctive RNA-binding properties although it has a similar fold as other ones. PubMed: 28735863DOI: 10.1016/j.bbrc.2017.07.104 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.49 Å) |
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