Structure of F1-ATPase from the obligate anaerobe Fusobacterium nucleatum

The crystal structure of the F 1 -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 1 -ATPases from Ca...

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Bibliographic Details
Published in:Open biology 2019-06, Vol.9 (6), p.190066-190066
Main Authors: Petri, Jessica, Nakatani, Yoshio, Montgomery, Martin G, Ferguson, Scott A, Aragão, David, Leslie, Andrew G W, Heikal, Adam, Walker, John E, Cook, Gregory M
Format: Article
Language:English
Subjects:
atp hydrolysis
catalytic f1-atpase
fusobacterium nucleatum
pathogen
regulation
structure
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Summary:The crystal structure of the F 1 -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 1 -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 E -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.
ISSN:2046-2441
DOI:10.1098/rsob.190066