Structure and mechanism of mRNA cap (guanine-N7) methyltransferase.
作者： Carme Fabrega , Stéphane Hausmann , Vincent Shen , Stewart Shuman , Christopher D Lima
DOI: 10.1016/S1097-2765(03)00522-7
关键词: Methylation 、 RNA capping 、 Biology 、 Guanine 、 Leaving group 、 Transferase 、 Biochemistry 、 Methyltransferase 、 Stereochemistry 、 Binding site 、 Protein structure
摘要: A suite of crystal structures is reported for a cellular mRNA cap (guanine-N7) methyltransferase in complex with AdoMet, AdoHcy, and the guanylate. Superposition ligand complexes suggests an in-line mechanism methyl transfer, albeit without direct contacts between enzyme either N7 atom guanine (the attacking nucleophile), carbon or sulfur AdoMet/AdoHcy leaving group). The indicate that catalysis methylation accomplished by optimizing proximity orientation substrates, assisted favorable electrostatic environment. enzyme-ligand structures, together new mutational data, fully account biochemical specificity guanine-N7 reaction, essential defining step eukaryotic synthesis.
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