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2bo5
From Proteopedia
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| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN
Overview
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.
About this Structure
2BO5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit., Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D, J Mol Biol. 2005 Aug 26;351(4):824-38. PMID:16045926
Page seeded by OCA on Thu Mar 20 16:04:30 2008
Categories: Bos taurus | H(+)-transporting two-sector ATPase | Single protein | Carbajo, R J. | Kellas, F A. | Montgomery, M G. | Neuhaus, D. | Runswick, M J. | Walker, J E. | Alpha-subunit | Atp synthase | Beta-subunit | Binding interface | Cf(1) | Chemical shift mapping | Chemical shift perturbation | Hydrogen ion transport | Hydrolase | Ion transport | Mitochondrion | Nmr | Oscp | Peripheral stalk | Protein-protein interaction | Titration | Transit peptide | Transport
