2jmx
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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 F(1)F(o)-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
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