ArticleJournal of molecular biology2009
Insights into tRNA-dependent amidotransferase evolution and catalysis from the structure of the Aquifex aeolicus enzyme.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.Chembiochem : a European journal of chemical biology · 2025Review
- Isolation and Characterization of Two Novel Genera of Jumbo Bacteriophages InfectingAntibiotics (Basel, Switzerland) · 2024Article
- Review
- Structural Computational Analysis of the Natural History of Class I aminoacyl-tRNA Synthetases Suggests their Role in Establishing the Genetic Code.Journal of molecular evolution · 2021Article
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Evolution of the genetic code.Transcription · 2021Review
- Pathogenic variants in glutamyl-tRNANature communications · 2018Article
- Computational analysis of ammonia transfer along two intramolecular tunnels in Staphylococcus aureus glutamine-dependent amidotransferase (GatCAB).The journal of physical chemistry. B · 2015Article
- Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases.Nucleic acids research · 2014Article
- The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate.PloS one · 2014Article
- A molecular pathway for the egress of ammonia produced by nitrogenase.Scientific reports · 2013Article
- Gates of enzymes.Chemical reviews · 2013Review
- Structure and function of allophanate hydrolase.The Journal of biological chemistry · 2013Article
- The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family.Biochemistry · 2013Article
- The kinase activity of the Helicobacter pylori Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase is sensitive to distal mutations in its putative ammonia tunnel.Biochemistry · 2012Article
- Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.Nature · 2010Article
- Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.The EMBO journal · 2010Article
- Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition.Nucleic acids research · 2010Article
- Structure of a tRNA-dependent kinase essential for selenocysteine decoding.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Many bacteria form Gln-tRNA(Gln) and Asn-tRNA(Asn) by conversion of the misacylated Glu-tRNA(Gln) and Asp-tRNA(Asn) species catalyzed by the GatCAB amidotransferase in the presence of ATP and an amide donor (glutamine or asparagine). Here, we report the crystal structures of GatCAB from the hyperthermophilic bacterium Aquifex aeolicus, complexed with glutamine, asparagine, aspartate, ADP, or ATP. In contrast to the Staphylococcus aureus GatCAB, the A. aeolicus enzyme formed acyl-enzyme intermediates with either glutamine or asparagine, in line with the equally facile use by the amidotransferase of these amino acids as amide donors in the transamidation reaction. A water-filled ammonia channel is open throughout the length of the A. aeolicus GatCAB from the GatA active site to the synthetase catalytic pocket in the B-subunit. A non-catalytic Zn(2+) site in the A. aeolicus GatB stabilizes subunit contacts and the ammonia channel. Judged from sequence conservation in the known GatCAB sequences, the Zn(2+) binding motif was likely present in the primordial GatB/E, but became lost in certain lineages (e.g., S. aureus GatB). Two divalent metal binding sites, one permanent and the other transient, are present in the catalytic pocket of the A. aeolicus GatB. The two sites enable GatCAB to first phosphorylate the misacylated tRNA substrate and then amidate the activated intermediate to form the cognate products, Gln-tRNA(Gln) or Asn-tRNA(Asn).
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