The Structural and Functional Connection between the Catalytic and Proton Translocating Sectors of the Mitochondrial F 1 F 0 -ATP Synthase |
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Authors: | Sergio Papa Fzaneo Zanotti Antonio Gaballo |
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Affiliation: | (1) Department of Medical Biochemistry and Biology, University of Bari, 70124 Bari, Italy;(2) Department of Medical Biochemistry and Biology, University of Bari, 70124 Bari, Italy;(3) Centre for the Study of Mitochondria and Energy Metabolism, Consiglio Nazionale delle Ricerche, University of Bari, Italy |
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Abstract: | The structural and functional connection between the peripheral catalytic F1 sector and theproton-translocating membrane sector F0 of the mitochondrial ATP synthase is reviewed. Theobservations examined show that the N-terminus of subunit , the carboxy-terminal and centralregion of F0I-PVP(b), OSCP, and part of subunit d constitute a continuous structure, the lateralstalk, which connects the peripheries of F1 to F0 and surrounds the central element of thestalk, constituted by subunits and . The ATPase inhibitor protein (IF1) binds at one sideof the F1F0 connection. The carboxy-terminal segment of IF1 apparently binds to OSCP. The42L-58K segment of IF1, which is per se the most active domain of the protein, binds at thesurface of one of the three / pairs of F1, thus preventing the cyclic interconversion of thecatalytic sites required for ATP hydrolysis. |
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Keywords: | F1F0-ATP synthase adenosine triphosphatase-inhibitor protein synthetic peptides OSCP |
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