1UAL
Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition
Summary for 1UAL
Entry DOI | 10.2210/pdb1ual/pdb |
Related | 1UAJ 1UAK 1UAM |
Descriptor | tRNA (Guanine-N(1)-)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total) |
Functional Keywords | methyltransferase, spout class, trmd, trna(m1g37)methyltransferase, trna modification, transferase |
Biological source | Haemophilus influenzae |
Cellular location | Cytoplasm (Potential): P43912 |
Total number of polymer chains | 1 |
Total formula weight | 31205.56 |
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 citation | Ahn, 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: 12773376DOI: 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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