Fig. 6: Cryo-EM reveals a unique binding pocket of LEI-800 within DNA gyrase. | Nature Chemistry

Fig. 6: Cryo-EM reveals a unique binding pocket of LEI-800 within DNA gyrase.

From: Discovery of isoquinoline sulfonamides as allosteric gyrase inhibitors with activity against fluoroquinolone-resistant bacteria

Fig. 6

a, An overview of the Gyr–Mu217–LEI-800 cryo-EM map depicted as an overlay of two different contour level maps. Low-resolution contour (white, 5σ) illustrates the position of GyrA CTDs and GyrB ATPase domains. The high-resolution part (12σ) is coloured according to the scheme: coral, GyrB; beige, GyrA; teal, DNA; golden, LEI-800. b, An overview of the model of the Gyr–Mu217–LEI-800 complex. GyrA (8–524) and GyrB (402–800) are depicted as beige and coral cartoon representations. The modelled 26-bp central part of Mu217 DNA is shown in teal. Two molecules of LEI-800 observed in a single gyrase heteroteramer are shown as golden van der Waals spheres. A uniform colour scheme is used throughout the manuscript. c, A Coulomb potential density map for LEI-800 (contoured at 12σ). d, A close-up of the horseshoe-like LEI-800 binding pocket on the DNA-binding surface of GyrA. GyrA is shown as molecular surface, DNA as cartoon representation and LEI-800 as van der Waals spheres.

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