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6.1.1.10: methionine-tRNA ligase

This is an abbreviated version!
For detailed information about methionine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.10

Reaction

ATP
+
L-methionine
 +
tRNAMet
=
AMP
 +
diphosphate
 +
L-methionyl-tRNAMet

Synonyms

hcMetRS, hmMetRS, let-65, MARS, mars-1, MetG, Methionine translase, Methionine--tRNA ligase, Methionyl tRNA synthetase, Methionyl-transfer ribonucleate synthetase, Methionyl-transfer ribonucleic acid synthetase, Methionyl-transfer RNA synthetase, methionyl-tRNA synthetase, methionyl-tRNA synthetase1, methionyl-tRNA-synthetase, MetRS, MetRS1, MetRS2, MetS, More, MRS, MRSapi, MRScyt, Synthetase, methionyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.10 methionine-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.10 - methionine-tRNA ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme-mitochondrial tRNAMet complex with or without methionyl sulfamoyl adenosine, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
enzyme in complex with inhibitors, sitting drop vapor diffusion method, using 0.2 M ammonium nitrate, 20% (wv)PEG-3350 pH 7.5 or 25% (w/v) PEG-1500, 100 mM MMT buffer, pH 5.0 or 25% (w/v) PEG-1500, 7% (w/v) PCB pH 4.0 or 0.2 Mammonium acetate, 0.1 M sodium acetate trihydrate, pH 4.6, 30% (w/v) PEG-4000
at 2.5 A resolution
-
crystal structure analysis, catalytic core, tertiary structure of the C-terminal tRNA-binding appendices determined by binding analysis of catalytically inactive tRNA homologous binding proteins: tRNA-binding protein 111 and endothelial monocyte-activating polypeptide II, i.e. EMAPII, comparison of structure with other aminoacyl tRNA synthetases from other organism
-
crystal structure determination by X-ray diffraction at 2.0 A resolution, 3D-structure of the C-terminally truncated enzyme, species-specific knuckle structures are determined
-
crystal structure of the tryptic fragment of the enzyme complexed with ATP, at 2.5 A resolution
-
crystals of active fragment of MW 64000 obtained by controlled proteolysis
-
crystals of purified free enzyme and enzyme complexed with L-methionine are diffused by several methionine analogues, i.e. L-difluoromethionine, L-trifluoromethionine, D,L-phosphomethionine and D,L-iodo-methionine, X-ray diffraction structure determination at 1.9 A resolution and analysis
purified enzyme complexed with L-methionine, protein solution: 8 mg/ml protein, 10 mM KH2PO4, pH 7.3, 10 mM 2-mercaptoethanol, initiating by microseeding with crystals from the free enzyme at 20°C, in 1.1 ammonium citrate, 0.5% v/v methyl-2,4-pentanediol, 0.6 mM L-methionine, 2 mM 2-mercaptoethanol, 30 mM phosphate buffer, pH 7.0, 1 day, X-ray diffraction structure determination at 1.8 A resolution, structure analysis and modeling
-
the crystal structure of the mutated MetRS is determined in the apo form as well as complexed with methionine or azidonorleucine to 1.4 to 1.7 A resolution
truncated form
-
purified recombinant His-tagged catalytic core of methionyl-tRNA synthetase, containing a 3C protease cleavage site, in complex with the substrates MgATP2- and methionine, and in complex with two products, methionyladenylate and pyrophosphate, along with a Mg2+ ion that bridges them, hanging drop vapor diffusion, room temperature, 0.002 ml of 22 mg/ml protein in 25 mM HEPES, pH 7.0, 0.5 M NaCl, 0.025% sodium azide, 5% glycerol, 1 mM TCEP, 0.01 mM ZnCl2, 10 mM MgATP2- and 10 mM L-methionine, is mixed with 0.002 ml of reservoir solution containing 0.2 M potassium formate or potassium nitrate, pH 7.0-7.5, and 24-28% PEG 3350, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
monomeric MetRS in complex with the ligands methionine and adenosine or with methionine, X-ray diffraction structure determination and analysis at 2.3 A and 2.8 A resolution, respectively
-
the structure of methionyl-tRNA synthetase is determined to a resolution of 2.1 A
hanging drop vapor diffusion method, using 30% (w/v) PEG 4000, 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate (pH 4.6)
C-terminal domain, hanging drop vapor diffusion method, using 20% (w/v) PEG8000 as precipitating agent in the presence of 50 mM potassium phosphate
purified recombinant M606 enzyme, hanging drop vapor diffusion method, from 0.1 M MES, pH 6.5, 3,5% PEG 6000, and 2% dioxane, 22°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution
recombinant 12 kDa protein 2, 20% PEG 8000, cryoprotection in 10% ethylene glycol, 50 mM KH2PO4, X-ray diffraction structure determination at 2.0 A, and analysis
purified recombinant MetRS-N-Arc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 8-14% PEG 20000, 1-3% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
purified recombinant MetRS-N–Arc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 8–14% PEG 20000, 1–3% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
crystal structure analysis, catalytic core, tertiary structure of the C-terminal tRNA-binding appendices determined by binding analysis of catalytically inactive tRNA homologous binding proteins: tRNA-binding protein 111 and endothelial monocyte-activating polypeptide II, i.e. EMAPII, comparison of structure with other aminoacyl tRNA synthetases from other organism
-
X-ray diffraction crystal structure determination at 2.0 A resolution and analysis
-
in complex with L-methionine and inhibitors, sitting drop vapor diffusion method, using 2.0-2.3 M (NH4)2SO4, 0.2 M NaCl, and 0.1 M sodium cacodylate (pH 6.0-6.6)
sitting drop vapor diffusion method, using 2.0-2.3 M (NH4)2SO4, 0.2 M NaCl and 0.1 M sodium cacodylate pH 6.2-6.8