How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit.

TitleHow the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit.
Publication TypeJournal Article
Year of Publication2007
AuthorsCarbajo, RJ, Kellas, FA, Yang, J-C, Runswick, MJ, Montgomery, MG, Walker, JE, Neuhaus, D
JournalJ Mol Biol
Volume368
Issue2
Pagination310-8
Date Published2007 Apr 27
ISSN0022-2836
KeywordsAdenosine Triphosphatases, Amino Acid Sequence, Animals, Carrier Proteins, Cattle, Membrane Proteins, Mitochondrial Proton-Translocating ATPases, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptides, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Structure-Activity Relationship, Thermodynamics
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.

DOI10.1016/j.jmb.2007.02.059
Alternate JournalJ. Mol. Biol.
Citation Key10.1016/j.jmb.2007.02.059
PubMed ID17355883
Grant ListMC_U105178934 / / Medical Research Council / United Kingdom
MC_U105663150 / / Medical Research Council / United Kingdom