3q87 | pdb_00003q87

Structure of eukaryotic translation termination complex methyltransferase Mtq2-Trm112

spinqualitylabelsall models 3q87, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q87 is a 2 chain structure with sequence from Encephalitozoon cuniculi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SAM, ZN Related: 2j6a Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein.,Liger D, Mora L, Lazar N, Figaro S, Henri J, Scrima N, Buckingham RH, van Tilbeurgh H, Heurgue-Hamard V, Graille M Nucleic Acids Res. 2011 Apr 7. PMID:21478168 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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