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Gene Review:

aspS - aspartyl-tRNA synthetase

Thermus thermophilus HB27

Berthet-Colominas, C. et al., Ng, J.D. et al., Logan, D.T. et al., Briand, C. et al.

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Disease relevance of TTC0359

The dimeric multidomain enzyme aspartyl-tRNA synthetase from Thermus thermophilus has been crystallized within dialysis reactors of the Advanced Protein Crystallization Facility in the laboratory on earth and under microgravity aboard the US Space Shuttle [1].

High impact information on TTC0359

As expected from primary sequence comparisons, there are remarkable similarities between the tertiary structures of asparaginyl-tRNA synthetase and aspartyl-tRNA synthetase, and most of the active site residues are identical except for three key differences [2].
Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems [3].

Biological context of TTC0359

The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site [4].

References

Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination. Ng, J.D., Sauter, C., Lorber, B., Kirkland, N., Arnez, J., Giegé, R. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid. Berthet-Colominas, C., Seignovert, L., Härtlein, M., Grotli, M., Cusack, S., Leberman, R. EMBO J. (1998) [Pubmed]
Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems. Briand, C., Poterszman, A., Mitschler, A., Yusupov, M., Thierry, J.C., Moras, D. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. Logan, D.T., Mazauric, M.H., Kern, D., Moras, D. EMBO J. (1995) [Pubmed]

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