F1-ATPase from Fusobacterium nucleatum

The catalytic head of the ATP-making motor from a disease-causing bacterium, and how it keeps itself in check.

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ATP synthase is the rotary motor that makes most of a cell’s ATP. Its F1 part, a ring of three α and three β subunits around a central stalk, can also run backwards and break ATP down, so cells keep that reverse reaction in check. This structure of F1 from Fusobacterium nucleatum, an anaerobic bacterium that causes disease in people, shows an enzyme that is only partly inhibited, and suggests that its activity is tuned by the amount of ADP around, as in our own mitochondria (paper).

The work was led by Greg Cook’s group in New Zealand with John Walker’s group at the MRC Mitochondrial Biology Unit in Cambridge (John Walker shared the 1997 Nobel Prize in Chemistry for his work on ATP synthase). The data were collected on MX2 at the Australian Synchrotron, and radiation damage meant merging four datasets from two crystals. The paper credits me with methodology and investigation.