{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["394(Pt 2)"],"submitter":["Liu Y"],"pubmed_abstract":["aaRSs (aminoacyl-tRNA synthetases) are responsible for the covalent linking of amino acids to their cognate tRNAs via the aminoacylation reaction and play a vital role in maintaining the fidelity of protein synthesis. LeuRS (leucyl-tRNA synthetase) can link not only the cognate leucine but also the nearly cognate residues Ile and Met to tRNA(Leu). The editing domain of LeuRS deacylates the mischarged Ile-tRNA(Leu) and Met-tRNA(Leu). We report here the crystal structures of ecLeuRS-ED (the editing domain of Escherichia coli LeuRS) in both the apo form and in complexes with Met and Ile at 2.0 A, 2.4 A, and 3.2 A resolution respectively. The editing active site consists of a number of conserved amino acids, which are involved in the precise recognition and binding of the noncognate amino acid"],"journal":["The Biochemical journal"],"pagination":["399-407"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1408670"],"repository":["biostudies-literature"],"pubmed_title":["Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination."],"pmcid":["PMC1408670"],"pubmed_authors":["Liao J","Liu Y","Zhu B","Ding J","Wang ED"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination.","description":"aaRSs (aminoacyl-tRNA synthetases) are responsible for the covalent linking of amino acids to their cognate tRNAs via the aminoacylation reaction and play a vital role in maintaining the fidelity of protein synthesis. LeuRS (leucyl-tRNA synthetase) can link not only the cognate leucine but also the nearly cognate residues Ile and Met to tRNA(Leu). The editing domain of LeuRS deacylates the mischarged Ile-tRNA(Leu) and Met-tRNA(Leu). We report here the crystal structures of ecLeuRS-ED (the editing domain of Escherichia coli LeuRS) in both the apo form and in complexes with Met and Ile at 2.0 A, 2.4 A, and 3.2 A resolution respectively. The editing active site consists of a number of conserved amino acids, which are involved in the precise recognition and binding of the noncognate amino acid","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Mar","modification":"2026-05-02T08:28:51.907Z","creation":"2025-05-29T21:46:31.928Z"},"accession":"S-EPMC1408670","cross_references":{"pubmed":["16277600"],"doi":["10.1042/BJ20051249","10.1042/bj20051249"]}}