Studies in the interaction of the tRNAPhe derivative bearing an arylazide group on its G24 residue with Escherichia coli ribosomes and tRNA-(adenine-l-)methyl transferase from Thermus thermophilus
نویسندگان
چکیده
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Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNA.
Methyltransferases from the m(1)A(58) tRNA methyltransferase (TrmI) family catalyze the S-adenosyl-l-methionine-dependent N(1)-methylation of tRNA adenosine 58. The crystal structure of Thermus thermophilus TrmI, in complex with S-adenosyl-l-homocysteine, was determined at 1.7 A resolution. This structure is closely related to that of Mycobacterium tuberculosis TrmI, and their comparison enable...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 1990
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.00027e