1GMJ

The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase

Summary for 1GMJ

• Entry DOI: 10.2210/pdb1gmj/pdb
• Related: 1HF9
• Descriptor: ATPASE INHIBITOR (1 entity in total)
• Functional Keywords: atpase inhibitor, bovine f1-atpase inhibitor protein, coiled-coil structure, p dependent oligomerization, atp hydrolysis
• Biological source: BOS TAURUS (BOVINE)
• Total number of polymer chains: 4
• Total formula weight: 38382.29

Authors

Cabezon, E.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2001-09-14, release date: 2002-01-01, Last modification date: 2024-05-08)

Primary citation

Cabezon, E.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E.
The Structure of Bovine If(1), the Regulatory Subunit of Mitochondrial F-ATPase.
Embo J., 20:6990-, 2001

PubMed Abstract: In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase.

PubMed: 11742976
DOI: 10.1093/EMBOJ/20.24.6990

Experimental method

X-RAY DIFFRACTION (2.2 Å)