6RKU

E. coli DNA Gyrase - DNA binding and cleavage domain in State 1

6RKU の概要

• エントリーDOI: 10.2210/pdb6rku/pdb
• EMDBエントリー: 4910
• 分子名称: DNA gyrase subunit A, DNA gyrase subunit B, DNA Strand 1, ... (5 entities in total)
• 機能のキーワード: isomerase, complex, dna gyrase, inhibitor, dna binding protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 394364.33

構造登録者

Vanden Broeck, A.,Lamour, V. (登録日: 2019-04-30, 公開日: 2019-11-06, 最終更新日: 2024-05-22)

主引用文献

Vanden Broeck, A.,Lotz, C.,Ortiz, J.,Lamour, V.
Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex.
Nat Commun, 10:4935-4935, 2019

PubMed Abstract: 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.

PubMed: 31666516
DOI: 10.1038/s41467-019-12914-y

実験手法

ELECTRON MICROSCOPY (4 Å)