7WM5

Crystal structure of apo TrmM from Mycoplasma capricolum

7WM5 の概要

• エントリーDOI: 10.2210/pdb7wm5/pdb
• 分子名称: Methyltransferase (2 entities in total)
• 機能のキーワード: t6a, m6a, methyltransferase, transferase
• 由来する生物種: Mycoplasma capricolum subsp. capricolum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30048.60

構造登録者

Jeong, H.,Kim, J. (登録日: 2022-01-14, 公開日: 2022-06-29, 最終更新日: 2023-11-29)

主引用文献

Jeong, H.,Lee, Y.,Kim, J.
Structural and functional characterization of TrmM in m 6 A modification of bacterial tRNA.
Protein Sci., 31:e4319-e4319, 2022

PubMed Abstract: N -methyladenosine (m A), widely distributed in both coding and noncoding RNAs, regulates the epigenetic signals and RNA metabolism in eukaryotes. Although this posttranscriptional modification is frequently observed in messenger and ribosomal RNA, it is relatively rare in transfer RNA. In Escherichia coli, TrmM encoded by yfiC is the tRNA-specific N methyltransferase, which modifies the A37 residue of tRNA (cmo UAC) using S-adenosyl-l-methionine as a methyl donor. However, the structure-function relationship of this enzyme is not completely understood. In this report, we determined two x-ray crystal structures of Mycoplasma capricolum TrmM with and without S-adenosyl-l-homocysteine, which is a reaction product. We also demonstrated the cellular and in vitro activities of this enzyme in the m A modification of tRNA and the requirement of a divalent metal ion for its function, which is unprecedented in other RNA N methyltransferases, including the E. coli TrmM. Our results reveal that the dimeric form of M. capricolum TrmM is important for efficient tRNA binding and catalysis, thereby offering insights into the distinct substrate specificity of the monomeric E. coli homolog.

PubMed: 35481631
DOI: 10.1002/pro.4319

実験手法

X-RAY DIFFRACTION (2.15 Å)