5DNO

Crystal structure of Mmi1 YTH domain complex with RNA

5DNO の概要

• エントリーDOI: 10.2210/pdb5dno/pdb
• 関連するPDBエントリー: 5DNP
• 分子名称: YTH domain-containing protein mmi1, RNA (5'-R(*CP*UP*UP*AP*AP*AP*C)-3') (3 entities in total)
• 機能のキーワード: rna-protein complex, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Schizosaccharomyces pombe 972h- (Fission yeast); 詳細
• 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: 22495.45

構造登録者

Wang, C.Y.,Zhu, Y.W.,Wu, J.H.,Shi, Y.Y. (登録日: 2015-09-10, 公開日: 2016-04-06, 最終更新日: 2023-11-08)

主引用文献

Wang, C.Y.,Zhu, Y.W.,Bao, H.Y.,Jiang, Y.Y.,Xu, C.,Wu, J.H.,Shi, Y.Y.
A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1
Nucleic Acids Res., 44:969-982, 2016

PubMed Abstract: The YTH domain-containing protein Mmi1, together with other factors, constitutes the machinery used to selectively remove meiosis-specific mRNA during the vegetative growth of fission yeast. Mmi1 directs meiotic mRNAs to the nuclear exosome for degradation by recognizing their DSR (determinant of selective removal) motif. Here, we present the crystal structure of the Mmi1 YTH domain in the apo state and in complex with a DSR motif, demonstrating that the Mmi1 YTH domain selectively recognizes the DSR motif. Intriguingly, Mmi1 also contains a potential m(6)A (N(6)-methyladenine)-binding pocket, but its binding of the DSR motif is dependent on a long groove opposite the m(6)A pocket. The DSR-binding mode is distinct from the m(6)A RNA-binding mode utilized by other YTH domains. Furthermore, the m(6)A pocket cannot bind m(6)A RNA. Our structural and biochemical experiments uncover the mechanism of the YTH domain in binding the DSR motif and help to elucidate the function of Mmi1.

PubMed: 26673708
DOI: 10.1093/nar/gkv1382

実験手法

X-RAY DIFFRACTION (1.8 Å)