1gmj
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| , resolution 2.2Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF BOVINE IF1, THE REGULATORY SUBUNIT OF MITOCHONDRIAL F-ATPASE
OverviewOverview
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.
About this StructureAbout this Structure
1GMJ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase., Cabezon E, Runswick MJ, Leslie AG, Walker JE, EMBO J. 2001 Dec 17;20(24):6990-6. PMID:11742976
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