PMID:7701318
| Citation |
Nureki, O, Vassylyev, DG, Katayanagi, K, Shimizu, T, Sekine, S, Kigawa, T, Miyazawa, T, Yokoyama, S and Morikawa, K (1995) Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Science 267:1958-65 |
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| Abstract |
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. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. 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. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases/chemistry; Anticodon; Biological Evolution; Computer Graphics; Crystallography, X-Ray; Escherichia coli/enzymology; Glutamate-tRNA Ligase/chemistry; Glutamate-tRNA Ligase/metabolism; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; RNA, Transfer, Glu/chemistry; RNA, Transfer, Glu/metabolism; Sequence Alignment; Thermus thermophilus/enzymology |
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