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tRNA ribose 2'-O-methyltransferase, aTrm56 This family is an aTrm56 that catalyzes the 2'-O-methylation of the cytidine residue in archaeal tRNA, using S-adenosyl-L-methionine. Biochemical assays showed that aTrm56 forms a dimer and prefers the L-shaped tRNA to the lambda form as its substrate. aTrm56 consists of the SPOUT domain, which contains the characteriztic deep trefoil knot for AdoMet binding, and a unique C-terminal beta-hairpin.
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