2jmx: Difference between revisions
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==Overview== | ==Overview== | ||
The peripheral stalk of ATP synthase acts as a stator holding the | The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) 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 alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
How the N-terminal | How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit., Carbajo RJ, Kellas FA, Yang JC, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D, J Mol Biol. 2007 Apr 27;368(2):310-8. Epub 2007 Feb 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17355883 17355883] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Carbajo, R | [[Category: Carbajo, R J.]] | ||
[[Category: Kellas, F | [[Category: Kellas, F A.]] | ||
[[Category: Montgomery, M | [[Category: Montgomery, M G.]] | ||
[[Category: Neuhaus, D.]] | [[Category: Neuhaus, D.]] | ||
[[Category: Runswick, M | [[Category: Runswick, M J.]] | ||
[[Category: Walker, J | [[Category: Walker, J E.]] | ||
[[Category: Yang, J.]] | [[Category: Yang, J.]] | ||
[[Category: oscp-nt alpha-nt complex]] | [[Category: oscp-nt alpha-nt complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:10 2008'' | ||
Revision as of 19:04, 21 February 2008
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OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase
OverviewOverview
The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) 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 alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide.
About this StructureAbout this Structure
2JMX is a Protein complex structure of sequences from Bos taurus. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit., Carbajo RJ, Kellas FA, Yang JC, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D, J Mol Biol. 2007 Apr 27;368(2):310-8. Epub 2007 Feb 22. PMID:17355883
Page seeded by OCA on Thu Feb 21 18:04:10 2008