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• W3033997412 endingPage "836" @default.
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• W3033997412 abstract "In contrast to most bacteria, the mycobacterial F1FO-ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) does not perform ATP hydrolysis-driven proton translocation. Although subunits α, γ and ε of the catalytic F1-ATPase component α3:β3:γ:ε have all been implicated in the suppression of the enzyme’s ATPase activity, the mechanism remains poorly defined. Here, we brought the central stalk subunit ε into focus by generating the recombinant Mycobacterium smegmatis F1-ATPase (MsF1-ATPase), whose 3D low-resolution structure is presented, and its ε-free form MsF1αβγ, which showed an eightfold ATP hydrolysis increase and provided a defined system to systematically study the segments of mycobacterial ε’s suppression of ATPase activity. Deletion of four amino acids at ε’s N terminus, mutant MsF1αβγεΔ2-5, revealed similar ATP hydrolysis as MsF1αβγ. Together with biochemical and NMR solution studies of a single, double, triple and quadruple N-terminal ε-mutants, the importance of the first N-terminal residues of mycobacterial ε in structure stability and latency is described. Engineering ε’s C-terminal mutant MsF1αβγεΔ121 and MsF1αβγεΔ103-121 with deletion of the C-terminal residue D121 and the two C-terminal ɑ-helices, respectively, revealed the requirement of the very C terminus for communication with the catalytic α3β3-headpiece and its function in ATP hydrolysis inhibition. Finally, we applied the tools developed during the study for an in silico screen to identify a novel subunit ε-targeting F-ATP synthase inhibitor." @default.
• W3033997412 created "2020-06-12" @default.
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• W3033997412 date "2020-07-04" @default.
• W3033997412 modified "2023-10-16" @default.
• W3033997412 title "A systematic assessment of mycobacterial F₁‐ATPase subunit ε’s role in latent ATPase hydrolysis" @default.
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• W3033997412 doi "https://doi.org/10.1111/febs.15440" @default.
• W3033997412 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32525613" @default.
• W3033997412 hasPublicationYear "2020" @default.
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