Flexible Recognition of the tRNA G18 Methylation Target Site by TrmH Methyltransferase through First Binding and Induced Fit Processes*
نویسندگان
چکیده
منابع مشابه
Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5.
Trm5 is a eukaryal and archaeal tRNA methyltransferase that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to the N(1) position of G37 directly 3' to the anticodon. While the biological role of m(1)G37 in enhancing translational fidelity is well established, the catalytic mechanism of Trm5 has remained obscure. To address the mechanism of Trm5 and more broadly the mechanism of N-m...
متن کاملMechanism of N-methylation by the tRNA mG37 methyltransferase Trm5
Trm5 is a eukaryal and archaeal tRNA methyltransferase that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to the N position of G37 directly 39 to the anticodon. While the biological role of mG37 in enhancing translational fidelity is well established, the catalytic mechanism of Trm5 has remained obscure. To address the mechanism of Trm5 and more broadly the mechanism of N-methyla...
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Induced fit explains why biomolecules can bind together even if they are not optimized for binding. However, induced fit can lead to a kinetic bottleneck and does not describe every interaction in the absence of prior complementarity. Preselection of a fitting conformer is an alternative to induced fit.
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Protozoan parasites are among the most devastating infectious agents of humans responsible for a variety of diseases including amebiasis, which is one of the three most common causes of death from parasitic disease. The agent of amebiasis is the amoeba parasite Entamoeba histolytica that exists under two stages: the infective cyst found in food or water and the invasive trophozoite living in th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m109.065698