Cloned (Comment) | Organism |
---|---|
recombinant expression of the N-terminally His-tagged AspRS | Entamoeba histolytica |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Entamoeba histolytica | 5829 | - |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Entamoeba histolytica | C4LZN0 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged AspRS, cleavage of the N-terminal His-tag | Entamoeba histolytica |
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 | ? | - |
? |
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 | Comment | Organism |
---|---|---|
Aspartyl-tRNA synthetase | - |
Entamoeba histolytica |
AspRS | - |
Entamoeba histolytica |
More | AspRS is a class IIb aminoacyl-tRNA synthetase | Entamoeba histolytica |