2BO5

Bovine oligomycin sensitivity conferral protein N-terminal domain

Summary for 2BO5

• Entry DOI: 10.2210/pdb2bo5/pdb
• NMR Information: BMRB: 6564
• Descriptor: ATP SYNTHASE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN (1 entity in total)
• Functional Keywords: atp synthase, peripheral stalk, oscp, alpha-subunit, beta-subunit, protein-protein interactions, chemical shift perturbations, chemical shift mapping, titration, binding interface, cf(1), hydrogen ion transport, hydrolase, ion transport, mitochondrion, transit peptide, transport
• Biological source: BOS TAURUS (BOVINE)
• Cellular location: Mitochondrion: P13621
• Total number of polymer chains: 1
• Total formula weight: 13240.51

Authors

Carbajo, R.J.,Kellas, F.A.,Runswick, M.J.,Montgomery, M.G.,Walker, J.E.,Neuhaus, D. (deposition date: 2005-04-07, release date: 2005-08-17, Last modification date: 2024-05-15)

Primary citation

Carbajo, R.J.,Kellas, F.A.,Runswick, M.J.,Montgomery, M.G.,Walker, J.E.,Neuhaus, D.
Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit.
J. Mol. Biol., 351:824-838, 2005

PubMed Abstract: The peripheral stalk of ATP synthase holds the alpha3beta3 catalytic subcomplex stationary against the torque of the rotating central stalk. 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 F1 subcomplex. Here we present the solution structure of OSCP-NT and an NMR titration study of its interaction with peptides representing N-terminal tails of F1 alpha-subunits. The structure comprises a bundle of six alpha-helices, and its interaction site contains adjoining hydrophobic surfaces of helices 1 and 5; residues in the region 1-8 of the alpha-subunit are essential for the interaction. The OSCP-NT is similar to the N-terminal domain of the delta-subunit from Escherichia coli ATP synthase (delta-NT), except that their surface charges differ (basic and acidic, respectively). As the charges of the adjacent crown regions in their alpha3beta3 complexes are similar, the OSCP-NT and delta-NT probably do not contact the crowns extensively. The N-terminal tails of alpha-subunit tails are probably alpha-helical, and so this interface, which is essential for the rotary mechanism of the enzyme, appears to consist of helix-helix interactions.

PubMed: 16045926
DOI: 10.1016/j.jmb.2005.06.012

Experimental method

SOLUTION NMR