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-Structure paper
タイトル | Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 4935, Year 2019 |
掲載日 | 2019年10月30日 |
著者 | Arnaud Vanden Broeck / Christophe Lotz / Julio Ortiz / Valérie Lamour / |
PubMed 要旨 | DNA gyrase is an essential enzyme involved in the homeostatic control of DNA supercoiling and the target of successful antibacterial compounds. Despite extensive studies, a detailed architecture of ...DNA gyrase is an essential enzyme involved in the homeostatic control of DNA supercoiling and the target of successful antibacterial compounds. Despite extensive studies, a detailed architecture of the full-length DNA gyrase from the model organism E. coli is still missing. Herein, we report the complete structure of the E. coli DNA gyrase nucleoprotein complex trapped by the antibiotic gepotidacin, using phase-plate single-particle cryo-electron microscopy. Our data unveil the structural and spatial organization of the functional domains, their connections and the position of the conserved GyrA-box motif. The deconvolution of two states of the DNA-binding/cleavage domain provides a better understanding of the allosteric movements of the enzyme complex. The local atomic resolution in the DNA-bound area reaching up to 3.0 Å enables the identification of the antibiotic density. Altogether, this study paves the way for the cryo-EM determination of gyrase complexes with antibiotics and opens perspectives for targeting conformational intermediates. |
リンク | Nat Commun / PubMed:31666516 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.0 - 6.6 Å |
構造データ | EMDB-4909, PDB-6rks: EMDB-4910, PDB-6rku: EMDB-4912, PDB-6rkv: EMDB-4913, PDB-6rkw: EMDB-4914: EMDB-4915: |
化合物 | ChemComp-JHN: ChemComp-ANP: |
由来 |
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キーワード | ISOMERASE / Complex / DNA Gyrase / Inhibitor / DNA BINDING PROTEIN |