NDLI: How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria

Content Provider	PubMed Central
Author	Gledhill, Jonathan R. Montgomery, Martin G. Leslie, Andrew G. W. Walker, John E.
Copyright Year	2007
Abstract	The structure of bovine F1-ATPase inhibited by a monomeric form of the inhibitor protein, IF1, known as I1–60His, lacking most of the dimerization region, has been determined at 2.1-Å resolution. The resolved region of the inhibitor from residues 8–50 consists of an extended structure from residues 8–13, followed by two α-helices from residues 14–18 and residues 21–50 linked by a turn. The binding site in the βDP-αDP catalytic interface is complex with contributions from five different subunits of F1-ATPase. The longer helix extends from the external surface of F1 via a deep groove made from helices and loops in the C-terminal domains of subunits βDP, αDP, βTP, and αTP to the internal cavity surrounding the central stalk. The linker and shorter helix interact with the γ-subunit in the central stalk, and the N-terminal region extends across the central cavity to interact with the nucleotide binding domain of the αE subunit. To form these complex interactions and penetrate into the core of the enzyme, it is likely that the initial interaction of the inhibitor with F1 forms via the open conformation of the βE subunit. Then, as two ATP molecules are hydrolyzed, the βE-αE interface converts to the βDP-αDP interface via the βTP-αTP interface, trapping the inhibitor progressively in its binding site and a nucleotide in the catalytic site of subunit βDP. The inhibition probably arises by IF1 imposing the structure and properties of the βTP-αTP interface on the βDP-αDP interface, thereby preventing it from hydrolyzing the bound ATP.
Related Links	http://dx.doi.org/10.1073/pnas.0707326104
Ending Page	15676
Page Count	6
Starting Page	15671
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	40
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-10-02
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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