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

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)