3Q87

Structure of E. cuniculi Mtq2-Trm112 complex responible for the methylation of eRF1 translation termination factor

3Q87 の概要

• エントリーDOI: 10.2210/pdb3q87/pdb
• 関連するPDBエントリー: 2J6A
• 分子名称: Putative uncharacterized protein ECU08_1170, N6 adenine specific DNA methylase, ZINC ION, ... (5 entities in total)
• 機能のキーワード: sam-methyltransferase, methyltransferase, methylation, transferase activator-transferase complex, transferase activator/transferase
• 由来する生物種: Encephalitozoon cuniculi; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33873.06

構造登録者

Liger, D.,Mora, L.,Lazar, N.,Figaro, S.,Henri, J.,Scrima, N.,Buckingham, R.H.,van Tilbeurgh, H.,Heurgue-Hamard, V.,Graille, M. (登録日: 2011-01-06, 公開日: 2011-05-18, 最終更新日: 2024-03-20)

主引用文献

Liger, D.,Mora, L.,Lazar, N.,Figaro, S.,Henri, J.,Scrima, N.,Buckingham, R.H.,van Tilbeurgh, H.,Heurgue-Hamard, V.,Graille, M.
Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein
Nucleic Acids Res., 2011

PubMed Abstract: Methylation is a common modification encountered in DNA, RNA and proteins. It plays a central role in gene expression, protein function and mRNA translation. Prokaryotic and eukaryotic class I translation termination factors are methylated on the glutamine of the essential and universally conserved GGQ motif, in line with an important cellular role. In eukaryotes, this modification is performed by the Mtq2-Trm112 holoenzyme. Trm112 activates not only the Mtq2 catalytic subunit but also two other tRNA methyltransferases (Trm9 and Trm11). To understand the molecular mechanisms underlying methyltransferase activation by Trm112, we have determined the 3D structure of the Mtq2-Trm112 complex and mapped its active site. Using site-directed mutagenesis and in vivo functional experiments, we show that this structure can also serve as a model for the Trm9-Trm112 complex, supporting our hypothesis that Trm112 uses a common strategy to activate these three methyltransferases.

PubMed: 21478168
DOI: 10.1093/nar/gkr176

実験手法

X-RAY DIFFRACTION (1.997 Å)