1wp0: Difference between revisions

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New page: left|200px<br /> <applet load="1wp0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wp0, resolution 2.8Å" /> '''Human SCO1'''<br /> ...
 
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[[Image:1wp0.gif|left|200px]]<br />
[[Image:1wp0.gif|left|200px]]<br /><applet load="1wp0" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1wp0" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1wp0, resolution 2.8&Aring;" />
caption="1wp0, resolution 2.8&Aring;" />
'''Human SCO1'''<br />
'''Human SCO1'''<br />


==Overview==
==Overview==
Human SCO1 and SCO2 are copper-binding proteins involved in the assembly, of mitochondrial cytochrome c oxidase (COX). We have determined the, crystal structure of the conserved, intermembrane space core portion of, apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including, thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding, ligands located at the same positions as the conserved catalytic residues, in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase, activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity, to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2, associated with fatal mitochondrial disorders, one lies in a highly, conserved exposed surface away from the copper-binding region, suggesting, that this region is involved in protein-protein interactions. These data, suggests that SCO functions not as a COX copper chaperone, but rather as a, mitochondrial redox signaling molecule.
Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. These data suggests that SCO functions not as a COX copper chaperone, but rather as a mitochondrial redox signaling molecule.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1WP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WP0 OCA].  
1WP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WP0 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Banting, G.S.]]
[[Category: Banting, G S.]]
[[Category: Glerum, D.M.]]
[[Category: Glerum, D M.]]
[[Category: Hendrickson, W.A.]]
[[Category: Hendrickson, W A.]]
[[Category: Schon, E.A.]]
[[Category: Schon, E A.]]
[[Category: Sue, C.]]
[[Category: Sue, C.]]
[[Category: Williams, J.C.]]
[[Category: Williams, J C.]]
[[Category: Yang, H.]]
[[Category: Yang, H.]]
[[Category: cu-binding protein]]
[[Category: cu-binding protein]]
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[[Category: redox]]
[[Category: redox]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:53:11 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:43 2008''