Literature summary for 2.1.1.220 extracted from

Kuratani, M.; Yanagisawa, T.; Ishii, R.; Matsuno, M.; Si, S.Y.; Katsura, K.; Ushikoshi-Nakayama, R.; Shibata, R.; Shirouzu, M.; Bessho, Y.; Yokoyama, S.
Crystal structure of tRNA m1A58 methyltransferase TrmI from Aquifex aeolicus in complex with S-adenosyl-L-methionine (2014), J. Struct. Funct. Genomics, 15, 173-180.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene aq_311, recombinant expression in Escherichia coli strain Rosetta (DE3)	Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, mixing of 0.001 ml of 10-12 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 150 mM NaCl, 1 mM DTT, and 2 mM S-adenosyl-L-methionine, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl buffer, pH 8.4, and 20% ethanol, at 20°C, cryoprotection in 0.1 M Tris-HCl buffer, pH 8.4, 20% ethanol, and 35% ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement method, using the coordinates of TrmI from Thermotoga maritima, PDB ID 1O54, as the starting model	Aquifex aeolicus

Crystallization (Comment)

Organism

purified enzyme in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, mixing of 0.001 ml of 10-12 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 150 mM NaCl, 1 mM DTT, and 2 mM S-adenosyl-L-methionine, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl buffer, pH 8.4, and 20% ethanol, at 20°C, cryoprotection in 0.1 M Tris-HCl buffer, pH 8.4, 20% ethanol, and 35% ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement method, using the coordinates of TrmI from Thermotoga maritima, PDB ID 1O54, as the starting model

Aquifex aeolicus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28700	-	x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation	Aquifex aeolicus
29000	-	x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation	Aquifex aeolicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + adenine58 in tRNA	Aquifex aeolicus	-	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O66653	gene aq_311	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain Rosetta (DE3) by heat treatment at 70°C for 30 min, anion exchange and hydrophobic interaction chromatography, and dialysis, followed by cation exchange chromatography, gel filtration, and ultrafiltration	Aquifex aeolicus

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
?	x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation	Aquifex aeolicus

Synonyms

Synonyms	Comment	Organism
TrmI	-	Aquifex aeolicus
tRNA m1A58 methyltransferase	-	Aquifex aeolicus

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Aquifex aeolicus

General Information

General Information	Comment	Organism
evolution	the N1-methyladenosine residue at position 58 of tRNA is found in the three domains of life	Aquifex aeolicus
physiological function	the N1-methyladenosine residue at position 58 of tRNA is found in the three domains of life, and contributes to the stability of the three-dimensional L-shaped tRNA structure. In thermophilic bacteria, this modificationis important for thermal adaptation, and is catalyzed by thetRNA m1A58 methyltransferase TrmI, using S-adenosyl-L-methionine as the methyl donor	Aquifex aeolicus