4U8T

Crystal structure of YTH domain of Zygosaccharomyces rouxii MRB1 protein in complex with N6-Methyladenosine RNA

4U8T の概要

• エントリーDOI: 10.2210/pdb4u8t/pdb
• 分子名称: ZYRO0G01672p, RNA (5'-R(*AP*GP*GP*(6MZ)P*CP*AP*U)-3') (3 entities in total)
• 機能のキーワード: n6-methyladenosine rna, yth rna binding domain, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Zygosaccharomyces rouxii; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 136818.51

構造登録者

Luo, S.,Tong, L. (登録日: 2014-08-04, 公開日: 2014-09-10, 最終更新日: 2024-10-30)

主引用文献

Luo, S.,Tong, L.
Molecular basis for the recognition of methylated adenines in RNA by the eukaryotic YTH domain.
Proc.Natl.Acad.Sci.USA, 111:13834-13839, 2014

PubMed Abstract: Methylation of the N6 position of selected internal adenines (m(6)A) in mRNAs and noncoding RNAs is widespread in eukaryotes, and the YTH domain in a collection of proteins recognizes this modification. We report the crystal structure of the splicing factor YT521-B homology (YTH) domain of Zygosaccharomyces rouxii MRB1 in complex with a heptaribonucleotide with an m(6)A residue in the center. The m(6)A modification is recognized by an aromatic cage, being sandwiched between a Trp and Tyr residue and with the methyl group pointed toward another Trp residue. Mutations of YTH domain residues in the RNA binding site can abolish the formation of the complex, confirming the structural observations. These residues are conserved in the human YTH proteins that also bind m(6)A RNA, suggesting a conserved mode of recognition. Overall, our structural and biochemical studies have defined the molecular basis for how the YTH domain functions as a reader of methylated adenines.

PubMed: 25201973
DOI: 10.1073/pnas.1412742111

実験手法

X-RAY DIFFRACTION (2.7 Å)