1WP0

Human SCO1

Summary for 1WP0

• Entry DOI: 10.2210/pdb1wp0/pdb
• Descriptor: SCO1 protein homolog (2 entities in total)
• Functional Keywords: cu-binding protein, mitochondrial assembly factor, redox, chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion: O75880
• Total number of polymer chains: 3
• Total formula weight: 57386.95

Authors

Williams, J.C.,Sue, C.,Banting, G.S.,Yang, H.,Glerum, D.M.,Hendrickson, W.A.,Schon, E.A. (deposition date: 2004-08-27, release date: 2005-01-18, Last modification date: 2024-11-06)

Primary citation

Williams, J.C.,Sue, C.,Banting, G.S.,Yang, H.,Glerum, D.M.,Hendrickson, W.A.,Schon, E.A.
Crystal Structure of Human SCO1: IMPLICATIONS FOR REDOX SIGNALING BY A MITOCHONDRIAL CYTOCHROME c OXIDASE "ASSEMBLY" PROTEIN
J.Biol.Chem., 280:15202-15211, 2005

PubMed Abstract: 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.

PubMed: 15659396
DOI: 10.1074/jbc.M410705200

Experimental method

X-RAY DIFFRACTION (2.8 Å)