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-[[Image:2ggt.gif|left|200px]]<br />
+[[Image:2ggt.gif|left|200px]]<br /><applet load="2ggt" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2ggt" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2ggt, resolution 2.40&Aring;" />
 '''Crystal structure of human SCO1 complexed with nickel.'''<br />
 ==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.
+The solution structures of apo, Cu(I), and Ni(II) human Sco1 have been, determined. The protein passes from an open and conformationally mobile, state to a closed and rigid conformation upon metal binding as shown by, electrospray ionization MS and NMR data. The metal ligands of Cu(I) are, two Cys residues of the CPXXCP motif and a His residue. The latter is, suitably located to coordinate the metal anchored by the two Cys residues., The coordination sphere of Ni(II) in solution is completed by another, ligand, possibly Asp. Crystals of the Ni(II) derivative were also obtained, with the Ni(II) ion bound to the same His residue and to the two oxidized, Cys residues of the CPXXCP motif. We propose that the various structures, solved here represent the various states of the protein in its functional, cycle and that the metal can be bound to the oxidized protein at a certain, stage. Although it now seems reasonable that Sco1, which is characterized, by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys, motif to act as a copper chaperone, the oxidized form of the nickel-bound, protein suggests that it may also maintain the thioredoxin function.
 ==Disease==
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 ==About this Structure==
-GGT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NI and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GGT OCA].
+GGT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Ni+Binding+Site+For+Residue+A+299'>AC1</scene>, <scene name='pdbsite=AC2:Ni+Binding+Site+For+Residue+B+299'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+A+300'>AC3</scene> and <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+B+301'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGT 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15659396 15659396]
+A hint for the function of human Sco1 from different structures., Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Mangani S, Martinelli M, Palumaa P, Wang S, Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8595-600. Epub 2006 May 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16735468 16735468]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
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 [[Category: redox]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:18:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:17:12 2008''