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Structural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for Inhibitors

2022; American Society for Microbiology; Volume: 66; Issue: 12 Linguagem: Inglês

10.1128/aac.01056-22

1098-6596

Chui Fann Wong, Wuan Geok Saw, Sandip Basak, Mio Sano, Hiroshi Ueno, Hwee Wen Kerk, Dennis Litty, Priya Ragunathan, Thomas Dick, Volker Müller, Hiroyuki Noji, Gerhard Grüber,

Amoebic Infections and Treatments

The F 1 F O -ATP synthase is required for the viability of tuberculosis (TB) and nontuberculous mycobacteria (NTM) and has been validated as a drug target. Here, we present the cryo-EM structures of the Mycobacterium smegmatis F 1 -ATPase and the F 1 F O -ATP synthase with different nucleotide occupation within the catalytic sites and visualize critical elements for latent ATP hydrolysis and efficient ATP synthesis.