Architectures of Class-Defining and Specific Domains of Glutamyl-tRNA Synthetase

• Osamu Nureki

• Dmitry G. Vassylyev

• Katsuo Katayanagi

• Toshiyuki Shimizu

• Shun-ichi Sekine

• Takanori Kigawa

• Tatsuo Miyazawa

• Shigeyuki Yokoyama

• Kosuke Morikawa

抄録

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 Å 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 α/β 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 β-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-α-helix architecture, an α-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.

収録刊行物

• Science

  Science 267 (5206), 1958-1965, 1995-03-31

  American Association for the Advancement of Science (AAAS)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1360018298136923776
• NII論文ID: 80008226223
• DOI: 10.1126/science.7701318
• ISSN: 10959203
• ISSN: 00368075
• Web Site: https://www.science.org/doi/pdf/10.1126/science.7701318
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