Extended Data Fig. 10: The evybactin binding pocket is concealed in the M. tuberculosis gyrase ‘ATPase open’ state.
From: Evybactin is a DNA gyrase inhibitor that selectively kills Mycobacterium tuberculosis
Structure of S. cerevisiae TOP2 bound to DNA and nonhydrolyzable ATP analog, illustrating the ‘ATPase closed’ conformation of type-II topoisomerases (left, PDBID: 4GFH55). The ATPase and transducer domains are colored yellow and light green, the nucleolytic core is illustrated in orange and blue, and DNA is shown in grey. Structure of M. tuberculosis gyrase in an ‘ATPase open’ state (right, PDBID: 6GAV38), in which the ATPase regions are folded down from the position shown at left. The binding site for evybactin is illustrated as a black outline and shown as a purple surface in the inset. The inset shows the loop within the GyrB ATPase domain that is specific to Corynebacteriales gyrases and how this loop occludes the evybactin binding site in the ‘ATPase open’ conformation of the enzyme.
