The mitochondrial ATP synthase inhibitor protein binds near the C-terminus of the F1 beta-subunit.
The specific, mitochondrial ATP synthase protein (IF1) was covalently cross-linked to its binding site on the catalytic sector of the enzyme (F1-ATPase). The cross-linked complex was selectively cleaved, leaving IF1 intact to facilitate the subsequent purification of the F1 fragment to which IF1 was cross-linked. This fragment was identified by sequence analysis as comprising residues 394-459 on the F1 beta-subunit, near the C-terminus. This finding is discussed in the light of secondary structure predictions for both IF1 and the F1 beta-subunit, and sequence homologies between mitochondrial and other ATP synthases.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D046911:Macromolecular Substances; D008929:Mitochondria, Heart / Q000201:enzymology; D011506:Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011804:Quinolines / Q000494:pharmacology; D000097795:ATPase Inhibitory Protein
D046911:Macromolecular Substances; D011506:Proteins; D006180:Proton-Translocating ATPases; D011804:Quinolines; D000097795:ATPase Inhibitory Protein; C000470:EEDQ