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Pathogenic mycobacteria pose a sustained threat to global human health. Recently, cytochrome  bcc  complexes have gained interest as targets for antibiotic drug development. However, there is currently no structural information for the cytochrome  bcc  complex from these pathogenic mycobacteria. Here, we report the structures of  Mycobacterium tuberculosis  cytochrome  bcc  alone (2.68 Å resolution) and in complex with clinical drug candidates Q203 (2.67 Å resolution) and TB47 (2.93 Å resolution) determined by single-particle cryo-electron microscopy.  M. tuberculosis  cytochrome  bcc  forms a dimeric assembly with endogenous menaquinone/menaquinol bound at the quinone/quinol-binding pockets. We observe Q203 and TB47 bound at the quinol-binding site and stabilized by hydrogen bonds with the side chains of  QcrB Thr 313  and  QcrB Glu 314 , residues that are conserved across pathogenic mycobacteria. These high-resolution images provide a basis for the design of new mycobacterial cytochrome  bcc  inhibitors that could be developed into broad-spectrum drugs to treat mycobacterial infections.

Structure of Mycobacterium tuberculosis cytochrome bcc in complex with Q203 and TB47, two anti-TB drug candidates