Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.1.1.220: tRNA (adenine58-N1)-methyltransferase

This is an abbreviated version!
For detailed information about tRNA (adenine58-N1)-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.220

Reaction

S-adenosyl-L-methionine
+
adenine58 in tRNA
=
S-adenosyl-L-homocysteine
 +
N1-methyladenine58 in tRNA

Synonyms

EC 2.1.1.36, Gcd10p, Gcd10p-Gcd14p, Gcd10pyGcd14p complex, Gcd14p, m1A58 MTase, m1A58 tRNA methyl-transferase, m1A58 tRNA methyltransferase, m1A58-methyltransferase, m1A58MTase, Rv2118c, Rv2118p, Trm6, TRM6-TRM61 holoenzyme, Trm61A, Trm61B, TRm61p, TRm6p, TrmI, tRNA (m1A58) methyltransferase, tRNA (m1A58) MTase, tRNA m(1)A58 methyltransferase, tRNA m1A58 methyltransferase, two component m1A58 tRNA methyl-transferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.220 tRNA (adenine58-N1)-methyltransferase

Crystallization

Crystallization on EC 2.1.1.220 - tRNA (adenine58-N1)-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
crystal structure of the human m1A58 MTase in complex with tRNALys3 (PDB ID 5CCB), and of human complex Trm6-Trm61 (PDB ID 2B25)
human enzyme tRNA m1A58 MTase in complex with human tRNA3Lys and cofactors S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, mixing of 0.001 ml of 4.8 mg/ml protein in 50 mM HEPES, pH 7.5, 0.0664 mM tRNA3Lys, 2 mM S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, and 1 mM MgCl2, with 0.001 ml of reservoir solution containing 0.1 M Na acetate, pH 4.8-5.0, 2% w/v PEG 4000 and 15% v/v methyl-2,4-pentanediol, 16°C, 4-7 days, X-ray diffraction structure determination and analysis at 2.2-4.0 A resolution, molecular replacement
TrmI-61 protein complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
crystal structure of Rv2118c in complex with S-adenosyl-L-methionine has been determined at 1.98 A resolution
TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.98 A resolution
-
TrmI protein complexed as tetramer with S-adenosyl-L-homocysteine or as monomer with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.05-2.6 A or 1.6 A resolution, respectively
-
crystal structure is available for heterotetrameric Trm6-Trm61A complex from Saccharomyces cerevisiae
P41814; P46959
purified recombinant His-tagged TRM6-TRM61 complex, from 0.1 M KCl, 0.1 M Tris-HCl, pH 8.0, 25% w/v PEG 2000 MME, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
-
purified recombinant wild-type and selenomethionine-labeled holoenzyme in apoform and complexed with S-adenosyl-L-methionine (SAM), mixing of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 300 mM NaCl, and 5 mM DTT, with a three-fold molecular excess of S-adenosyl-L-methionine, sitting drop vapour diffusion method, with the mother liquor containing 0.1 M HEPES, PH 7.5, 2% v/v 2-methyl-2,4-pentanediol, 10% w/v PEG 6000, 3 days X-ray diffraction structure determination and analysis
P41814; P46959
ligand-free TrmI, X-ray diffraction structure determination and analysis at 1.65 A resolution
-
purified enzyme mutant D170A and Y78A in complex with S-adenosyl-L-methionine, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, 100 mM KCl, and 2mM S-adenosyl-L-methionine with reservoir solution containing 2.4 M ammonium sulfate and 10% v/v isopropanol for mutant D170A and 2.1 M ammonium sulfate and 8% v/v isopropanol for mutant Y78A, X-ray diffraction structure determination and analysis at 3.1 A and 2.6 A resolution, respectively. Crystallization assays of enzyme TrmI Y194A lead to poorly diffracting crystals
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
TrmI protein complexed with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 1.7 A resolution
-