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5EIP

apo-structure of YTH domain of SpMmi1

5EIP の概要
エントリーDOI10.2210/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
Wu, B.X.,Xu, J.H.,Su, S.C.,Ma, J.B. (登録日: 2015-10-30, 公開日: 2016-01-27, 最終更新日: 2024-03-20)
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: 28735863
DOI: 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)
構造検証レポート
Validation report summary of 5eip
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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