3Q87

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

Summary for 3Q87

• Entry DOI: 10.2210/pdb3q87/pdb
• Related: 2J6A
• Descriptor: Putative uncharacterized protein ECU08_1170, N6 adenine specific DNA methylase, ZINC ION, ... (5 entities in total)
• Functional Keywords: sam-methyltransferase, methyltransferase, methylation, transferase activator-transferase complex, transferase activator/transferase
• Biological source: Encephalitozoon cuniculi; More
• Total number of polymer chains: 2
• Total formula weight: 33873.06

Authors

Liger, D.,Mora, L.,Lazar, N.,Figaro, S.,Henri, J.,Scrima, N.,Buckingham, R.H.,van Tilbeurgh, H.,Heurgue-Hamard, V.,Graille, M. (deposition date: 2011-01-06, release date: 2011-05-18, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.997 Å)