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Literature summary for 6.1.1.10 extracted from

  • Larson, E.T.; Kim, J.E.; Zucker, F.H.; Kelley, A.; Mueller, N.; Napuli, A.J.; Verlinde, C.L.; Fan, E.; Buckner, F.S.; Van Voorhis, W.C.; Merritt, E.A.; Hol, W.G.
    Structure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphate (2011), Biochimie, 93, 570-582.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of the His-tagged catalytic core of MetRS in Escherichia coli using the expression vector AVA0421 Leishmania major

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Leishmania major

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required. The Mg2+ ion has six atoms arranged in a square bipyramidal coordination shell and bridges the diphosphate and MetAMP products. It is interacting with two oxygen atoms from two different phosphoryl groups of the diphosphate, one oxygen from the MetAMP phosphoryl group, and three water molecules, though one of these is a bit distant for a typical Mg2+ ligand at approximately 2.5 A Leishmania major
Zn2+ required Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Leishmania major
-
AMP + diphosphate + L-methionyl-tRNAMet
-
?

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged catalytic core of MetRS from Escherichia coli using the expression vector AVA0421 by nickel affinity chromatography and gel filtration Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
-
Leishmania major AMP + diphosphate + L-methionyl-tRNAMet
-
?
ATP + L-methionine + tRNAMet binding structures of substrates and products, overview Leishmania major AMP + diphosphate + L-methionyl-tRNAMet
-
?

Subunits

Subunits Comment Organism
More structure of LmMetRS in complex with two products, methionyladenylate and diphosphate, along with a Mg2+ ion that bridges them, the residues of the class I aaRS signature sequence motifs, KISKS and HIGH, make numerous contacts with the diphosphate, structure comparisons, overview Leishmania major

Synonyms

Synonyms Comment Organism
methionyl-tRNA synthetase
-
Leishmania major
MetRS
-
Leishmania major
More the enzyme belongs to the class I aminoacyl-tRNA synthetases Leishmania major

Cofactor

Cofactor Comment Organism Structure
ATP as MgATP2- Leishmania major