1ual
From Proteopedia
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Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition
Overview
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.
About this Structure
1UAL is a Single protein structure of sequence from Haemophilus influenzae with SAH as ligand. Active as tRNA (guanine-N(1)-)-methyltransferase, with EC number 2.1.1.31 Full crystallographic information is available from OCA.
Reference
Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition., Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK, EMBO J. 2003 Jun 2;22(11):2593-603. PMID:12773376
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