2bo5
From Proteopedia
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| - | [[Image:2bo5.gif|left|200px]] | + | [[Image:2bo5.gif|left|200px]] |
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| - | '''BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN''' | + | {{Structure |
| + | |PDB= 2bo5 |SIZE=350|CAPTION= <scene name='initialview01'>2bo5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BO5 is a [ | + | 2BO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. |
==Reference== | ==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:[http:// | + | 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]] | ||
[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
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[[Category: cf(1)]] | [[Category: cf(1)]] | ||
[[Category: chemical shift mapping]] | [[Category: chemical shift mapping]] | ||
| - | [[Category: chemical shift | + | [[Category: chemical shift perturbation]] |
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: oscp]] | [[Category: oscp]] | ||
[[Category: peripheral stalk]] | [[Category: peripheral stalk]] | ||
| - | [[Category: protein-protein | + | [[Category: protein-protein interaction]] |
[[Category: titration]] | [[Category: titration]] | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:30 2008'' |
Revision as of 14:04, 20 March 2008
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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
