6Q45

F1-ATPase from Fusobacterium nucleatum

Summary for 6Q45

• Entry DOI: 10.2210/pdb6q45/pdb
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (8 entities in total)
• Functional Keywords: complex, fusobacterium, hydrolase, atpase
• Biological source: Fusobacterium nucleatum subsp. nucleatum ATCC 25586; More
• Total number of polymer chains: 16
• Total formula weight: 730309.26

Authors

Petri, J.,Nakatani, Y.,Montgomery, M.G.,Ferguson, S.A.,Aragao, D.,Leslie, A.G.W.,Heikal, A.,Walker, J.E.,Cook, G.M. (deposition date: 2018-12-05, release date: 2019-07-10, Last modification date: 2024-02-07)

Primary citation

Petri, J.,Nakatani, Y.,Montgomery, M.G.,Ferguson, S.A.,Aragao, D.,Leslie, A.G.W.,Heikal, A.,Walker, J.E.,Cook, G.M.
Structure of F1-ATPase from the obligate anaerobe Fusobacterium nucleatum.
Open Biology, 9:190066-190066, 2019

PubMed 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.

PubMed: 31238823
DOI: 10.1098/rsob.190066

Experimental method

X-RAY DIFFRACTION (3.6 Å)