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L-arginine recognition by yeast arginyl-tRNA synthetase
J Cavarelli1, B Delagoutte, G Eriani
1UPR 9004 Biologie Structurale, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 163, 67404 Illkirch Cedex, France.
The EMBO Journal
|September 16, 1998
Summary
The crystal structure of yeast arginyl-tRNA synthetase (ArgRS) reveals how it binds L-arginine. This structure provides insights into aminoacyl-tRNA synthetase (aaRS) function and classification.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Arginyl-tRNA synthetase (ArgRS) is a class I aminoacyl-tRNA synthetase (aaRS) essential for protein synthesis.
- Understanding ArgRS structure is crucial for elucidating its catalytic mechanism and substrate specificity.
Purpose of the Study:
- To determine the crystal structure of Saccharomyces cerevisiae ArgRS bound to L-arginine.
- To analyze the interactions between ArgRS and L-arginine at the active site.
- To provide a framework for classifying class I aaRS.
Main Methods:
- X-ray crystallography to solve the crystal structure of ArgRS at 2.75 A resolution.
- Refinement of the crystal structure to a crystallographic R-factor of 19.7%.
Main Results:
- The ArgRS structure is predominantly alpha-helical, divided into five domains, including the class I-specific active site.
- L-arginine binding does not require tRNAArg, and all its hydrogen bond-forming capabilities are utilized for specific recognition.
- Key residues, including a conserved tyrosine, are involved in L-arginine binding and are conserved across ArgRS sequences.
Conclusions:
- The solved ArgRS structure reveals specific L-arginine binding mechanisms.
- The findings offer a new framework for sequence alignments and subclass definitions within class I aaRSs.
- This structural information advances our understanding of protein synthesis fidelity.