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- W1584043988 abstract "The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strains VK.-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 Å resolution (space group P212121, a = 61.4 Å, b = 156.1 Å, c = 177.3 Å) are routinely obtained. The same crystals have previously been described as crystals of threonyl-tRNA synthetase [1]." @default.
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- W1584043988 date "1993-07-05" @default.
- W1584043988 modified "2023-10-18" @default.
- W1584043988 title "Sequence, overproduction and crystallization of aspartyl-tRNA synthetase fromThermus thermophilus" @default.
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- W1584043988 doi "https://doi.org/10.1016/0014-5793(93)81069-c" @default.
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