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Literature summary extracted from

  • Barraud, P.; Golinelli-Pimpaneau, B.; Atmanene, C.; Sanglier, S.; Van Dorsselaer, A.; Droogmans, L.; Dardel, F.; Tisne, C.
    Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNA (2008), J. Mol. Biol., 377, 535-550.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.220 sitting-drop vapor-diffusion method at 19°C. Crystal structure of TrmI, in complex with S-adenosyl-L-homocysteine, is determined at 1.7 A resolution. The conserved residues that form the catalytic cavity (D170, Y78, and Y194) are essential for fashioning an optimized shape of the catalytic pocket Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.220 Thermus thermophilus Q8GBB2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Thermus thermophilus S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.220 tetramer the enzyme remains tetrameric upon tRNA binding, with formation of complexes involving one to two molecules of tRNA per TrmI tetramer Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
2.1.1.220 m1A58 tRNA methyltransferase
-
 Thermus thermophilus
2.1.1.220 TrmI
-
 Thermus thermophilus
2.1.1.220 tRNA m1A58 methyltransferase
-
 Thermus thermophilus