Structure of the ATP synthase from <i>Mycobacterium smegmatis</i> provides targets for treating tuberculosis.

ABSTRACT: The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a "fai

SUBMITTER: Montgomery MG 

PROVIDER: S-EPMC8617483 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature