The structure of bovine F1-ATPase in complex with its regulatory protein IF1.

TitleThe structure of bovine F1-ATPase in complex with its regulatory protein IF1.
Publication TypeJournal Article
Year of Publication2003
AuthorsCabezon, E, Montgomery, MG, Leslie, AGW, Walker, JE
JournalNat Struct Biol
Volume10
Issue9
Pagination744-50
Date Published2003 Sep
ISSN1072-8368
KeywordsAdenosine Triphosphate, Animals, Cattle, Crystallography, X-Ray, Dimerization, Hydrolysis, Mitochondria, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Proteins, Proton-Translocating ATPases
Abstract

In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.

DOI10.1038/nsb966
Alternate JournalNat. Struct. Biol.
Citation Key10.1038/nsb966
PubMed ID12923572