Binding of the inhibitor protein IF(1) to bovine F(1)-ATPase.

ABSTRACT: In the structure of bovine F(1)-ATPase inhibited with residues 1-60 of the bovine inhibitor protein IF(1), the α-helical inhibitor interacts with five of the nine subunits of F(1)-ATPase. In order to understand the contributions of individual amino acid residues to this complex binding mode, N-terminal deletions and point mutations have been introduced, and the binding properties of each mutant inhibitor protein have been examined. The N-terminal region of IF(1) destabilizes the interaction of the inhibitor with F(1)-ATPase and may assist in removing the inhibitor from its binding site when F(1)F(o)-ATPase is making ATP. Binding energy is provided by hydrophobic interactions between residues in the long α-helix of IF(1) and the C-terminal domains of the β(DP)-subunit and β(TP)-subunit and

SUBMITTER: Bason JV 

PROVIDER: S-EPMC3041923 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature