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2bo5

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[[Image:2bo5.gif|left|200px]]
[[Image:2bo5.gif|left|200px]]
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{{Structure
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|PDB= 2bo5 |SIZE=350|CAPTION= <scene name='initialview01'>2bo5</scene>
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The line below this paragraph, containing "STRUCTURE_2bo5", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span>
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{{STRUCTURE_2bo5| PDB=2bo5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo5 OCA], [http://www.ebi.ac.uk/pdbsum/2bo5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bo5 RCSB]</span>
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'''BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN'''
'''BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN'''
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16045926 16045926]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16045926 16045926]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: H(+)-transporting two-sector ATPase]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carbajo, R J.]]
[[Category: Carbajo, R J.]]
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[[Category: Runswick, M J.]]
[[Category: Runswick, M J.]]
[[Category: Walker, J E.]]
[[Category: Walker, J E.]]
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[[Category: alpha-subunit]]
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[[Category: Alpha-subunit]]
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[[Category: atp synthase]]
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[[Category: Atp synthase]]
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[[Category: beta-subunit]]
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[[Category: Beta-subunit]]
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[[Category: binding interface]]
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[[Category: Binding interface]]
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[[Category: cf(1)]]
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[[Category: Chemical shift mapping]]
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[[Category: chemical shift mapping]]
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[[Category: Chemical shift perturbation]]
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[[Category: chemical shift perturbation]]
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[[Category: Hydrogen ion transport]]
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[[Category: hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: hydrolase]]
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[[Category: Ion transport]]
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[[Category: ion transport]]
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[[Category: Mitochondrion]]
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[[Category: mitochondrion]]
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[[Category: Nmr]]
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[[Category: nmr]]
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[[Category: Oscp]]
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[[Category: oscp]]
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[[Category: Peripheral stalk]]
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[[Category: peripheral stalk]]
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[[Category: Protein-protein interaction]]
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[[Category: protein-protein interaction]]
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[[Category: Titration]]
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[[Category: titration]]
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[[Category: Transit peptide]]
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[[Category: transit peptide]]
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[[Category: Transport]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:33:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:09:15 2008''
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Revision as of 17:33, 3 May 2008

Image:2bo5.gif

Template:STRUCTURE 2bo5

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 Sat May 3 20:33:35 2008

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