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1wp0

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[[Image:1wp0.gif|left|200px]]
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{{STRUCTURE_1wp0| PDB=1wp0 | SCENE= }}
{{STRUCTURE_1wp0| PDB=1wp0 | SCENE= }}
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'''Human SCO1'''
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===Human SCO1===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15659396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15659396}}
==About this Structure==
==About this Structure==
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[[Category: Mitochondrial assembly factor]]
[[Category: Mitochondrial assembly factor]]
[[Category: Redox]]
[[Category: Redox]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:21:18 2008''

Revision as of 12:21, 29 July 2008

Template:STRUCTURE 1wp0

Human SCO1

Template:ABSTRACT PUBMED 15659396

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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