1wp0
From Proteopedia
(New page: 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=" | + | |
caption="1wp0, resolution 2.8Å" /> | caption="1wp0, resolution 2.8Å" /> | ||
'''Human SCO1'''<br /> | '''Human SCO1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human SCO1 and SCO2 are copper-binding proteins involved in the assembly | + | 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:// | + | 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 | + | [[Category: Banting, G S.]] |
| - | [[Category: Glerum, D | + | [[Category: Glerum, D M.]] |
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
| - | [[Category: Schon, E | + | [[Category: Schon, E A.]] |
[[Category: Sue, C.]] | [[Category: Sue, C.]] | ||
| - | [[Category: Williams, J | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:43 2008'' |
Revision as of 13:46, 21 February 2008
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Human SCO1
Contents |
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.
Disease
Known diseases associated with this structure: Hepatic failure, early onset, and neurologic disorder OMIM:[603644]
About this Structure
1WP0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein., Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA, J Biol Chem. 2005 Apr 15;280(15):15202-11. Epub 2005 Jan 19. PMID:15659396
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