Literature summary for 2.1.1.220 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q8GBB2	-	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
m1A58 tRNA methyltransferase	-	Thermus thermophilus
TrmI	-	Thermus thermophilus
tRNA m1A58 methyltransferase	-	Thermus thermophilus

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Release 2023.1 (January 2023)