Crystal structure of tRNA(m(1)G37)methyltransferase: insights into tRNA recognition

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tRNA(m(1)G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-l- methionine (AdoMet) to G(37) within a subset of bacterial tRNA species, which have a G residue at the 36th position. The modified 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 influenzae, 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 first 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.
Publisher
WILEY
Issue Date
2003-06
Language
English
Article Type
Article
Citation

EMBO JOURNAL, v.22, no.11, pp.2593 - 2603

ISSN
0261-4189
DOI
10.1093/emboj/cdg269
URI
http://hdl.handle.net/10203/295181
Appears in Collection
BS-Journal Papers(저널논문)
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