2ggt
|
Crystal structure of human SCO1 complexed with nickel.
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Hepatic failure, early onset, and neurologic disorder OMIM:[603644]
About this StructureAbout this Structure
2GGT is a Single protein structure of sequence from Homo sapiens with NI and CL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Nov 12 22:18:34 2007