Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2188663 | Journal of Molecular Biology | 2007 | 9 Pages |
Abstract
The peripheral stalk of ATP synthase acts as a stator holding the α3β3 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 α subunits of the F1 subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1–25 of the α-subunit of bovine F1-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the α-peptide.
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Authors
Rodrigo J. Carbajo, Fiona A. Kellas, Ji-Chun Yang, Michael J. Runswick, Martin G. Montgomery, John E. Walker, David Neuhaus,