Abstract
The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) catalytic subcomplex and the membrane subunit a against the torque of the rotating central stalk and attached c ring. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide.
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism*
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Cattle
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism*
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Mitochondrial Proton-Translocating ATPases / chemistry*
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Mitochondrial Proton-Translocating ATPases / metabolism*
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Peptides / chemistry
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / chemistry*
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Protein Subunits / metabolism*
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Structure-Activity Relationship
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Thermodynamics
Substances
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Carrier Proteins
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Membrane Proteins
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Peptides
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Protein Subunits
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Adenosine Triphosphatases
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Mitochondrial Proton-Translocating ATPases
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oligomycin sensitivity-conferring protein