{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["112(13)"],"submitter":["Tworowski D"],"pubmed_abstract":["At the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge of discrimination between cognate phenylalanine and closely similar noncognate tyrosine. Resampling of Tyr-tRNA(Phe) to PheRS increasing the number of correctly charged tRNA molecules has recently been revealed. Thus, the very same editing site of PheRS promotes hydrolysis of misacylated tRNA species, associated both with cis- and trans-editing pathways. Here we report the crystal structure of Thermus thermophilus PheRS (TtPheRS) at 2.6 Å resolution, in complex with phenylalanine and antibiotic puromycin mimicking the A76 of tRNA acylated with tyrosine. Starting from the complex structure and using a hybrid quantum mechanics/molecular mechanics approach, we investigate the pathways of e"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["3967-72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4386372"],"repository":["biostudies-literature"],"pubmed_title":["Universal pathway for posttransfer editing reactions: insights from the crystal structure of TtPheRS with puromycin."],"pmcid":["PMC4386372"],"pubmed_authors":["Safro MG","Moor N","Peretz M","Tworowski D","Klipcan L"],"additional_accession":[]},"is_claimable":false,"name":"Universal pathway for posttransfer editing reactions: insights from the crystal structure of TtPheRS with puromycin.","description":"At the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge of discrimination between cognate phenylalanine and closely similar noncognate tyrosine. Resampling of Tyr-tRNA(Phe) to PheRS increasing the number of correctly charged tRNA molecules has recently been revealed. Thus, the very same editing site of PheRS promotes hydrolysis of misacylated tRNA species, associated both with cis- and trans-editing pathways. Here we report the crystal structure of Thermus thermophilus PheRS (TtPheRS) at 2.6 Å resolution, in complex with phenylalanine and antibiotic puromycin mimicking the A76 of tRNA acylated with tyrosine. Starting from the complex structure and using a hybrid quantum mechanics/molecular mechanics approach, we investigate the pathways of e","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Mar","modification":"2026-04-17T23:17:30.647Z","creation":"2025-07-28T03:05:55.247Z"},"accession":"S-EPMC4386372","cross_references":{"pubmed":["25775602"],"doi":["10.1073/pnas.1414852112"]}}