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. 2023 Jan 23;6(1):52–67. doi: 10.1038/s41929-022-00904-1

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a, Scheme of GyrA and GyrB domains. The DNA cleavage–reunion complex is shown, along with the catalytic residue (Tyr122) and residues involved in quinolone resistance (GyrB Lys447 and Asp426 and GyrA Ser83 and Asp87). A consistent colour code is used throughout the manuscript: beige, GyrA; coral, GyrB. b, Chemical structure of albicidin. c, An overview of the Gyr–Mu217–albicidin cryo-EM map depicted as an overlay of two different contour level maps. Low-resolution contour (white) illustrates the position of GyrA CTDs and GyrB ATPase domains. High-resolution core part, including albicidin (in the zoomed-in image), is coloured according to the scheme in a: coral, GyrB; beige, GyrA; teal, DNA; yellow, albicidin. d, Cartoon representation of the overall model.