ArticleThe Journal of biological chemistry2014
Cocrystal structures of glycyl-tRNA synthetase in complex with tRNA suggest multiple conformational states in glycylation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
- Aminoacyl-tRNA-dependent enzymes in natural product biosynthesis: structure-function insights.The Journal of antibiotics · 2026Review
- Glycine Drives IMP Production in Hybrid Bream (Megalobrama Amblycephala ♀ × Culter Alburnus ♂) Via Concerted Action: Activating glycyl-tRNA Synthetase and Fueling the Pentose Phosphate Pathway.Marine biotechnology (New York, N.Y.) · 2026Article
- Binding of Glycyl-tRNA synthetase to Mengovirus RNA stimulates translation.Nucleic acids research · 2026Article
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Physiological and Metabolic Responses of Mongolian Horses to a 20 km Endurance Exercise and Screening for New Oxidative-Imbalance Biomarkers.Animals : an open access journal from MDPI · 2025Article
- Glycyl-tRNA sequestration is a unifying mechanism underlying GARS1-associated peripheral neuropathy.Nucleic acids research · 2025Article
- Article
- Enzymic recognition of amino acids drove the evolution of primordial genetic codes.Nucleic acids research · 2024Article
- Structural basis of a two-step tRNA recognition mechanism for plastid glycyl-tRNA synthetase.Nucleic acids research · 2023Article
- Fraisinib: a calixpyrrole derivative reducing A549 cell-derived NSCLC tumorFrontiers in pharmacology · 2023Article
- Pathogenic missense variants altering codon 336 of GARS1 lead to divergent dominant phenotypes.Human mutation · 2022Article
- Personalized Medicine in Mitochondrial Health and Disease: Molecular Basis of Therapeutic Approaches Based on Nutritional Supplements and Their Analogs.Molecules (Basel, Switzerland) · 2022Review
- Aminoacyl-tRNA synthetases in Charcot-Marie-Tooth disease: A gain or a loss?Journal of neurochemistry · 2021Review
- Mitochondrial Aminoacyl-tRNA Synthetase and Disease: The Yeast Contribution for Functional Analysis of Novel Variants.International journal of molecular sciences · 2021Review
- Article
- The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases.Scientific reports · 2020Article
- GARS-related disease in infantile spinal muscular atrophy: Implications for diagnosis and treatment.American journal of medical genetics. Part A · 2020Article
- Genetic and Clinical Features in 24 Chinese Distal Hereditary Motor Neuropathy Families.Frontiers in neurology · 2020Article
- Allele-specific RNA interference prevents neuropathy in Charcot-Marie-Tooth disease type 2D mouse models.The Journal of clinical investigation · 2019Article
- Neurodegenerative Charcot-Marie-Tooth disease as a case study to decipher novel functions of aminoacyl-tRNA synthetases.The Journal of biological chemistry · 2019Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charges tRNA molecules with cognate amino acids for protein synthesis. Glycyl-tRNA synthetase (GlyRS) is one of the most intriguing aminoacyl-tRNA synthetases due to its divergent quaternary structure and abnormal charging properties. In the past decade, mutations of human GlyRS (hGlyRS) were also found to be associated with Charcot-Marie-Tooth disease. However, the mechanisms of traditional and alternative functions of hGlyRS are poorly understood due to a lack of studies at the molecular basis. In this study we report crystal structures of wild type and mutant hGlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. The cocrystal structures suggest that insertions 1 and 3 work together with the active site in a cooperative manner to facilitate efficient substrate binding. Both the enzyme and tRNA molecules undergo significant conformational changes during glycylation. A working model of multiple conformations for hGlyRS catalysis is proposed based on the crystallographic and biochemical studies. This study provides insights into the catalytic pathway of hGlyRS and may also contribute to our understanding of Charcot-Marie-Tooth disease.
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