| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2030106 | Structure | 2006 | 9 Pages |
SummaryGlutamyl-tRNA synthetase (GluRS) is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation. We analyzed the role of tRNA in amino acid recognition by crystallography. In the GluRS•tRNAGlu•Glu structure, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site. This collaborative site is functional, as it is formed in the same manner in pretransition-state mimic, GluRS•tRNAGlu•ATP•Eol (a glutamate analog), and posttransition-state mimic, GluRS•tRNAGlu•ESA (a glutamyl-adenylate analog) structures. In contrast, in the GluRS•Glu structure, only GluRS forms the amino acid-binding site, which is defective and accounts for the binding of incorrect amino acids, such as D-glutamate and L-glutamine. Therefore, tRNAGlu is essential for formation of the completely functional binding site for L-glutamate. These structures, together with our previously described structures, reveal that tRNA plays a crucial role in accurate positioning of both L-glutamate and ATP, thus driving the amino acid activation.
