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Literature summary for 6.1.1.19 extracted from

  • Bi, K.; Zheng, Y.; Gao, F.; Dong, J.; Wang, J.; Wang, Y.; Gong, W.
    Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition (2014), Protein Cell, 5, 151-159.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 50 mM HEPES (pH 7.2), 100 mM sodium acetate, 22% (w/v) PEG 3350 Escherichia coli

Protein Variants

Protein Variants Comment Organism
D118A the mutation results in a 2fold increase in binding affinity Escherichia coli
D317A inactive Escherichia coli
R324A inactive Escherichia coli
Y313A the mutation results in a merely 2fold reduction in binding affinity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-arginine + tRNAArg Escherichia coli
-
 AMP + diphosphate + L-arginyl-tRNAArg
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P11875
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-NTA affinity resin column chromatography and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + tRNAArg
-
 Escherichia coli AMP + diphosphate + L-arginyl-tRNAArg
-
 ?

Synonyms

Synonyms Comment Organism
Arginyl-tRNA synthetase
-
 Escherichia coli
ArgRS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli