1OHH

BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1

Summary for 1OHH

• Entry DOI: 10.2210/pdb1ohh/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1GMJ 1H8E 1H8H 1HF9 1NBM 1QO1
• Descriptor: ATP synthase subunit alpha, mitochondrial, ATP synthase subunit beta, mitochondrial, ATP synthase subunit gamma, mitochondrial, ... (6 entities in total)
• Functional Keywords: synthase, atp phosphorylase, atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase
• Biological source: Bos taurus (Bovine); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P01096
• Total number of polymer chains: 8
• Total formula weight: 363619.85

Authors

Cabezon, E.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2003-05-27, release date: 2003-06-09, Last modification date: 2023-12-13)

Primary citation

Cabezon, E.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E.
The Structure of Bovine F1-ATPase in Complex with its Regulatory Protein If1
Nat.Struct.Biol., 10:744-, 2003

PubMed 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.

PubMed: 12923572
DOI: 10.1038/NSB966

Experimental method

X-RAY DIFFRACTION (2.8 Å)