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1UAL

Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition

Summary for 1UAL
Entry DOI10.2210/pdb1ual/pdb
Related1UAJ 1UAK 1UAM
DescriptortRNA (Guanine-N(1)-)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
Functional Keywordsmethyltransferase, spout class, trmd, trna(m1g37)methyltransferase, trna modification, transferase
Biological sourceHaemophilus influenzae
Cellular locationCytoplasm (Potential): P43912
Total number of polymer chains1
Total formula weight31205.56
Authors
Ahn, H.J.,Kim, H.-W.,Yoon, H.-J.,Lee, B.I.,Suh, S.W.,Yang, J.K. (deposition date: 2003-03-11, release date: 2003-06-17, Last modification date: 2023-12-27)
Primary citationAhn, H.J.,Kim, H.-W.,Yoon, H.-J.,Lee, B.I.,Suh, S.W.,Yang, J.K.
Crystal structure of tRNA(m(1)G37)methyltransferase: insights into tRNA recognition
EMBO J., 22:2593-2603, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12773376
DOI: 10.1093/emboj/cdg269
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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