biostudies-literatureTabagari NEuropean Research Council100132https://www.ebi.ac.uk/biostudies/studies/S-EPMC12268091biostudies-literatureUnknown12Proteins are heteropolymers composed of twenty standard amino acids, but over 500 non-proteogenic amino acids exist in nature that can be misincorporated into proteins. Canavanine is an antimetabolite of the chemically similar L-arginine. It can be utilized by bacteria such as <i>Pseudomonas canavaninivorans</i> in the legume rhizome as a sole source of carbon and nitrogen. However, canavanine misincorporates in proteins of this bacterium as its arginyl-tRNA synthetase loads tRNA^Arg with both canavanine and arginine. Canavanyl-tRNA^Arg deacetylase (CtdA) removes canavanine from misloaded tRNA^Arg, preventing its protein toxicity, being the first enzyme known to edit tRNA mischarged with a non-proteinogenic amino acid. We have elucidated CtdA's crystal structuJournal of structural biology: XIndel-driven evolution of the canavanine tRNA-editing deacetylase enzyme CtdA.PMC12268091681777Hartig JSHauth FMayans OTabagari NFleming JRfalseIndel-driven evolution of the canavanine tRNA-editing deacetylase enzyme CtdA.Proteins are heteropolymers composed of twenty standard amino acids, but over 500 non-proteogenic amino acids exist in nature that can be misincorporated into proteins. Canavanine is an antimetabolite of the chemically similar L-arginine. It can be utilized by bacteria such as <i>Pseudomonas canavaninivorans</i> in the legume rhizome as a sole source of carbon and nitrogen. However, canavanine misincorporates in proteins of this bacterium as its arginyl-tRNA synthetase loads tRNA^Arg with both canavanine and arginine. Canavanyl-tRNA^Arg deacetylase (CtdA) removes canavanine from misloaded tRNA^Arg, preventing its protein toxicity, being the first enzyme known to edit tRNA mischarged with a non-proteinogenic amino acid. We have elucidated CtdA's crystal structu2025-01-01T00:00:00Z2025 Dec2026-03-16T07:55:15.327Z2025-08-15T03:06:27.968ZS-EPMC122680914068762010.1016/j.yjsbx.2025.100132