{"doi":"10.1073/pnas.2407398121","title":"Structural basis of chiral wrap and T-segment capture by\n                    <i>Escherichia coli</i>\n                    DNA gyrase","abstract":"<jats:p>\n                    Type II topoisomerase DNA gyrase transduces the energy of ATP hydrolysis into the negative supercoiling of DNA. The postulated catalytic mechanism involves stabilization of a chiral DNA loop followed by the passage of the T-segment through the temporarily cleaved G-segment resulting in sign inversion. The molecular basis for this is poorly understood as the chiral loop has never been directly observed. We have obtained high-resolution cryoEM structures of\n                    <jats:italic>Escherichia coli</jats:italic>\n                    gyrase with chirally wrapped 217 bp DNA with and without the fluoroquinolone moxifloxacin (MFX). Each structure constrains a positively supercoiled figure-of-eight DNA loop stabilized by a GyrA β-pinwheel domain which has the structure of a flat disc. By comparing the catalytic site of the native drug-free and MFX-bound gyrase structures both of which contain a single metal ion, we demonstrate that the enzyme is observed in a native precatalytic state. Our data imply that T-segment trapping is not dependent on the dimerization of the ATPase domains which appears to only be possible after strand passage has taken place.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2024,"id":674558,"datarank":0.4335557636844247,"base_score":2.8903717578961645,"endowment":2.8903717578961645,"self_citation_contribution":0.4335557636844247,"citation_network_contribution":0.0,"self_endowment_contribution":0.4335557636844247,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":17,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1762478,"name":"Zuzanna Pakosz-Stępień","orcid":"0000-0002-2288-8616","position":1,"is_corresponding":false},{"id":1762479,"name":"Jonathon D. Liston","orcid":"0000-0003-0283-8889","position":2,"is_corresponding":false},{"id":1762480,"name":"Olivia Gittins","orcid":"0000-0002-3818-3952","position":3,"is_corresponding":false},{"id":1762481,"name":"Marta Pabis","orcid":"0000-0001-7394-5206","position":4,"is_corresponding":false},{"id":881672,"name":"Jonathan G. Heddle","orcid":"0000-0003-0994-9928","position":5,"is_corresponding":false},{"id":1762482,"name":"Dmitry Ghilarov","orcid":"0000-0001-9325-3207","position":6,"is_corresponding":false},{"id":1762477,"name":"Elizabeth Michalczyk","orcid":"0000-0002-9276-7764","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"citation_network_status":"fetched"},"created_at":"2026-08-16T17:19:32.361937Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}