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Literature summary for 6.1.1.23 extracted from

  • Merritt, E.A.; Arakaki, T.L.; Larson, E.T.; Kelley, A.; Mueller, N.; Napuli, A.J.; Zhang, L.; Deditta, G.; Luft, J.; Verlinde, C.L.; Fan, E.; Zucker, F.; Buckner, F.S.; Van Voorhis, W.C.; Hol, W.G.
    Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica (2010), Mol. Biochem. Parasitol., 169, 95-100.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the N-terminally His-tagged AspRS Entamoeba histolytica

Crystallization (Commentary)

Crystallization (Comment) Organism
purified AspRS, sitting drop vapour diffusion method, 0.0002 ml of 9 mg/ml protein is mixed with 0.0002 ml of reservoir solution containing 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 5.5, and 23% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.8 A resolution Entamoeba histolytica

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
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Entamoeba histolytica 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Entamoeba histolytica AspRS must perform two sequential reactions. The first reaction is the formation of aspartyladenylate from the free amino acid and ATP, releasing diphosphate. The second reaction is the displacement of the adenylate moiety by the 3'-OH of the terminal adenosine of the tRNAAsp acceptor arm, yielding the covalently linked Asp-tRNAAsp. The active site must therefore bind the two initial reactants, Asp and ATP, and also provide access for the properly positioned acceptor stem of a bound tRNA molecule ?
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?

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica C4LZN0
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged AspRS, cleavage of the N-terminal His-tag Entamoeba histolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AspRS must perform two sequential reactions. The first reaction is the formation of aspartyladenylate from the free amino acid and ATP, releasing diphosphate. The second reaction is the displacement of the adenylate moiety by the 3'-OH of the terminal adenosine of the tRNAAsp acceptor arm, yielding the covalently linked Asp-tRNAAsp. The active site must therefore bind the two initial reactants, Asp and ATP, and also provide access for the properly positioned acceptor stem of a bound tRNA molecule Entamoeba histolytica ?
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?

Subunits

Subunits Comment Organism
homodimer structure modelling, overview Entamoeba histolytica
More AspRS is a class IIb aminoacyl-tRNA synthetase showing conserved structural features, overview Entamoeba histolytica

Synonyms

Synonyms Comment Organism
Aspartyl-tRNA synthetase
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Entamoeba histolytica
AspRS
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Entamoeba histolytica
More AspRS is a class IIb aminoacyl-tRNA synthetase Entamoeba histolytica