Structure of F-ATPase from the obligate anaerobe Fusobacterium nucleatum.

TitleStructure of F-ATPase from the obligate anaerobe Fusobacterium nucleatum.
Publication TypeJournal Article
Year of Publication2019
AuthorsPetri, J, Nakatani, Y, Montgomery, MG, Ferguson, SA, Aragão, D, Leslie, AGW, Heikal, A, Walker, JE, Cook, GM
JournalOpen Biol
Volume9
Issue6
Pagination190066
Date Published2019 Jun 28
ISSN2046-2441
Abstract

The crystal structure of the F-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.

DOI10.1098/rsob.190066
Alternate JournalOpen Biol
Citation Key10.1098/rsob.190066
PubMed ID31238823
PubMed Central IDPMC6597759
Grant ListMC_EX_MR/M009858/1 / / Medical Research Council / United Kingdom