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Literature summary for 6.1.1.7 extracted from

  • Smal, C.; Zanzoni, S.; D'Onofrio, M.; Molinari, H.; Cicero, D.; Assfalg, M.
    1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov (2014), Biomol. NMR Assign., 8, 415-418 .
    View publication on PubMed
Search for more literature for 6.1.1.7

Cloned(Commentary)

Cloned (Comment) Organism
gene alaS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His6-tagged full-length enzyme and C-terminal domain C-Ala in Escherichia coli strain BL21(DE3) Bizionia argentinensis

Organism

Organism UniProt Comment Textmining
Bizionia argentinensis G2EA49 isolated from surface seawater in Antarctica
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Bizionia argentinensis JUB59 G2EA49 isolated from surface seawater in Antarctica
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Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged full-length enzyme and C-terminal domain C-Ala from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, followed by tag cleavage through TEV protease, tag and TEV protease are removed by another turn of nickel affinity chromatography, and ultrafiltration and dialysis Bizionia argentinensis

Subunits

Subunits Comment Organism
More the enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Enzyme secondary structure prediction, overview Bizionia argentinensis

Synonyms

Synonyms Comment Organism
alanyltRNA synthetase
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 Bizionia argentinensis
AlaRS
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 Bizionia argentinensis

General Information

General Information Comment Organism
evolution the enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Alanyl-tRNA synthetases (AlaRSs) belong to class-II aminoacyl-tRNA synthetases Bizionia argentinensis
additional information the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from Bizionia argentinensis is determined, enzyme structure homology modeling using the X-ray structure of Aquifex aeolicus AlaRS C-Ala domain Bizionia argentinensis
physiological function alanyl-tRNA synthetases (AlaRSs) play an essential role in the early events of protein synthesis by catalyzing the conjugation of amino acids to their cognate transfer RNAs. The C-terminal domain, C-Ala, plays an essential role in enzyme activity Bizionia argentinensis