1GLN

ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE

Summary for 1GLN

• Entry DOI: 10.2210/pdb1gln/pdb
• Descriptor: GLUTAMYL-TRNA SYNTHETASE (2 entities in total)
• Functional Keywords: riken structural genomics/proteomics initiative, rsgi, structural genomics, aminoacyl-trna synthase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm : P27000
• Total number of polymer chains: 1
• Total formula weight: 53979.73

Authors

Nureki, O.,Vassylyev, D.G.,Katayanagi, K.,Shimizu, T.,Sekine, S.,Kigawa, T.,Miyazawa, T.,Yokoyama, S.,Morikawa, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1994-07-20, release date: 1995-10-15, Last modification date: 2024-02-07)

Primary citation

Nureki, O.,Vassylyev, D.G.,Katayanagi, K.,Shimizu, T.,Sekine, S.,Kigawa, T.,Miyazawa, T.,Yokoyama, S.,Morikawa, K.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
Science, 267:1958-1965, 1995

PubMed 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.

PubMed: 7701318

Experimental method

X-RAY DIFFRACTION (2.5 Å)