6H2V

Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase at 2.5A resolution

6H2V の概要

• エントリーDOI: 10.2210/pdb6h2v/pdb
• 分子名称: Methyltransferase-like protein 5, Multifunctional methyltransferase subunit TRM112-like protein, S-ADENOSYLMETHIONINE, ... (8 entities in total)
• 機能のキーワード: rrna maturation, methyltransferase, translation, ribosome synthesis, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 79685.67

構造登録者

van Tran, N.,Graille, M. (登録日: 2018-07-16, 公開日: 2019-07-31, 最終更新日: 2024-11-06)

主引用文献

van Tran, N.,Ernst, F.G.M.,Hawley, B.R.,Zorbas, C.,Ulryck, N.,Hackert, P.,Bohnsack, K.E.,Bohnsack, M.T.,Jaffrey, S.R.,Graille, M.,Lafontaine, D.L.J.
The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112.
Nucleic Acids Res., 47:7719-7733, 2019

PubMed Abstract: N6-methyladenosine (m6A) has recently been found abundantly on messenger RNA and shown to regulate most steps of mRNA metabolism. Several important m6A methyltransferases have been described functionally and structurally, but the enzymes responsible for installing one m6A residue on each subunit of human ribosomes at functionally important sites have eluded identification for over 30 years. Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with TRMT112, a known methyltransferase activator, to gain metabolic stability in cells. We provide the first atomic resolution structure of METTL5-TRMT112, supporting that its RNA-binding mode differs distinctly from that of other m6A RNA methyltransferases. On the basis of similarities with a DNA methyltransferase, we propose that METTL5-TRMT112 acts by extruding the adenosine to be modified from a double-stranded nucleic acid.

PubMed: 31328227
DOI: 10.1093/nar/gkz619

実験手法

X-RAY DIFFRACTION (2.49 Å)