2jmx: Difference between revisions

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New page: left|200px<br /><applet load="2jmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jmx" /> '''OSCP-NT (1-120) in complex with N-terminal (...
 
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[[Image:2jmx.gif|left|200px]]<br /><applet load="2jmx" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2jmx.gif|left|200px]]<br /><applet load="2jmx" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2jmx" />
caption="2jmx" />
'''OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase'''<br />
'''OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase'''<br />
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==About this Structure==
==About this Structure==
2JMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JMX OCA].  
2JMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMX OCA].  


==Reference==
==Reference==
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[[Category: oscp-nt alpha-nt complex]]
[[Category: oscp-nt alpha-nt complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:38:10 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:35:22 2008''

Revision as of 16:35, 23 January 2008

File:2jmx.gif


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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