1EFW

Crystal structure of aspartyl-tRNA synthetase from Thermus thermophilus complexed to tRNAasp from Escherichia coli

Summary for 1EFW

• Entry DOI: 10.2210/pdb1efw/pdb
• Descriptor: ASPARTYL-TRNA, ASPARTYL-TRNA SYNTHETASE (3 entities in total)
• Functional Keywords: aspartyl-trna synthetase, trna, protein-rna complex, ligase/rna, ligase-rna complex
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 179698.10

Authors

Briand, C.,Poterszman, A.,Eiler, S.,Webster, G.,Thierry, J.-C.,Moras, D. (deposition date: 2000-02-10, release date: 2000-06-19, Last modification date: 2025-03-19)

Primary citation

Briand, C.,Poterszman, A.,Eiler, S.,Webster, G.,Thierry, J.,Moras, D.
An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
J.Mol.Biol., 299:1051-1060, 2000

PubMed Abstract: The crystal structures of aspartyl-tRNA synthetase (AspRS) from Thermus thermophilus, a prokaryotic class IIb enzyme, complexed with tRNA(Asp) from either T. thermophilus or Escherichia coli reveal a potential intermediate of the recognition process. The tRNA is positioned on the enzyme such that it cannot be aminoacylated but adopts an overall conformation similar to that observed in active complexes. While the anticodon loop binds to the N-terminal domain of the enzyme in a manner similar to that of the related active complexes, its aminoacyl acceptor arm remains at the entrance of the active site, stabilized in its intermediate conformational state by non-specific interactions with the insertion and catalytic domains. The thermophilic nature of the enzyme, which manifests itself in a very low kinetic efficiency at 17 degrees C, the temperature at which the crystals were grown, is in agreement with the relative stability of this non-productive conformational state. Based on these data, a pathway for tRNA binding and recognition is proposed.

PubMed: 10843857
DOI: 10.1006/jmbi.2000.3819

Experimental method

X-RAY DIFFRACTION (3 Å)