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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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gltX  -  glutamyl-tRNA synthetase

Thermus thermophilus HB27

 
 
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Disease relevance of TTC0070

  • The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution [1].
 

High impact information on TTC0070

  • These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA [1].
  • In this study, we determined the crystal structure of the 'non-productive' complex of Thermus thermophilus GluRS, ATP and L-glutamate, together with those of the GluRS.ATP, GluRS.tRNA.ATP and GluRS.tRNA.GoA (a glutamyl-AMP analog) complexes [2].
  • In the absence of tRNA(Glu), ATP is accommodated in a 'non-productive' subsite within the ATP-binding site, so that the ATP alpha-phosphate and the glutamate alpha-carboxyl groups in GluRS [2].
 

Associations of TTC0070 with chemical compounds

  • Accordingly, such a conformation change of tRNAGlu in the complex with GluRS is required for the specific binding of L-glutamate as the substrate [3].

References

  1. Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Nureki, O., Vassylyev, D.G., Katayanagi, K., Shimizu, T., Sekine, S., Kigawa, T., Miyazawa, T., Yokoyama, S., Morikawa, K. Science (1995) [Pubmed]
  2. ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. Sekine, S., Nureki, O., Dubois, D.Y., Bernier, S., Chênevert, R., Lapointe, J., Vassylyev, D.G., Yokoyama, S. EMBO J. (2003) [Pubmed]
  3. Conformation change of tRNAGlu in the complex with glutamyl-tRNA synthetase is required for the specific binding of L-glutamate. Hara-Yokoyama, M., Yokoyama, S., Miyazawa, T. Biochemistry (1986) [Pubmed]
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