contributed equally to this work tRNA(m 1 G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-Lmethionine (AdoMet) to G 37 within a subset of bacterial tRNA species, which have a G residue at the 36th position. The modi®ed guanosine is adjacent to and 3¢ of the anticodon and is essential for the maintenance of the correct reading frame during translation. Here we report four crystal structures of TrmD from Haemophilus in¯uenzae, as binary complexes with either AdoMet or S-adenosyl-L-homocysteine (AdoHcy), as a ternary complex with AdoHcy and phosphate, and as an apo form. This ®rst structure of TrmD indicates that it functions as a dimer. It also suggests the binding mode of G 36 G 37 in the active site of TrmD and the catalytic mechanism. The N-terminal domain has a trefoil knot, in which AdoMet or AdoHcy is bound in a novel, bent conformation. The C-terminal domain shows structural similarity to trp repressor. We propose a plausible model for the TrmD 2 ±tRNA 2 complex, which provides insights into recognition of the general tRNA structure by TrmD.
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