1wp0

From Proteopedia

(Difference between revisions)

Revision as of 12:29, 6 January 2015

Human SCO1

Structural highlights

1wp0 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[SCO1_HUMAN] Defects in SCO1 are a cause of mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]; also known as cytochrome c oxidase deficiency. A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, excercise intolerance, developmental delay, delayed motor development and mental retardation. A subset of patients manifest Leigh syndrome.^[1] ^[2]

Function

[SCO1_HUMAN] Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX.^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leary SC, Cobine PA, Kaufman BA, Guercin GH, Mattman A, Palaty J, Lockitch G, Winge DR, Rustin P, Horvath R, Shoubridge EA. The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. Cell Metab. 2007 Jan;5(1):9-20. PMID:17189203 doi:10.1016/j.cmet.2006.12.001
↑ Valnot I, Osmond S, Gigarel N, Mehaye B, Amiel J, Cormier-Daire V, Munnich A, Bonnefont JP, Rustin P, Rotig A. Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy. Am J Hum Genet. 2000 Nov;67(5):1104-9. Epub 2000 Sep 28. PMID:11013136 doi:10.1016/S0002-9297(07)62940-1
↑ Leary SC, Cobine PA, Kaufman BA, Guercin GH, Mattman A, Palaty J, Lockitch G, Winge DR, Rustin P, Horvath R, Shoubridge EA. The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. Cell Metab. 2007 Jan;5(1):9-20. PMID:17189203 doi:10.1016/j.cmet.2006.12.001
↑ Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA. Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J Biol Chem. 2005 Apr 15;280(15):15202-11. Epub 2005 Jan 19. PMID:15659396 doi:10.1074/jbc.M410705200
↑ Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Mangani S, Martinelli M, Palumaa P, Wang S. A hint for the function of human Sco1 from different structures. Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8595-600. Epub 2006 May 30. PMID:16735468
↑ Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA. Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J Biol Chem. 2005 Apr 15;280(15):15202-11. Epub 2005 Jan 19. PMID:15659396 doi:10.1074/jbc.M410705200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wp0"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1wp0]] is a 3 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WP0 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wp0 RCSB], [http://www.ebi.ac.uk/pdbsum/1wp0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wp0 RCSB], [http://www.ebi.ac.uk/pdbsum/1wp0 PDBsum]</span></td></tr>
-<table>
+</table>
 == Disease ==
 [[http://www.uniprot.org/uniprot/SCO1_HUMAN SCO1_HUMAN]] Defects in SCO1 are a cause of mitochondrial complex IV deficiency (MT-C4D) [MIM:[http://omim.org/entry/220110 220110]]; also known as cytochrome c oxidase deficiency. A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, excercise intolerance, developmental delay, delayed motor development and mental retardation. A subset of patients manifest Leigh syndrome.<ref>PMID:17189203</ref> <ref>PMID:11013136</ref>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Banting, G S.]]
+[[Category: Banting, G S]]
-[[Category: Glerum, D M.]]
+[[Category: Glerum, D M]]
-[[Category: Hendrickson, W A.]]
+[[Category: Hendrickson, W A]]
-[[Category: Schon, E A.]]
+[[Category: Schon, E A]]
-[[Category: Sue, C.]]
+[[Category: Sue, C]]
-[[Category: Williams, J C.]]
+[[Category: Williams, J C]]
-[[Category: Yang, H.]]
+[[Category: Yang, H]]
 [[Category: Chaperone]]
 [[Category: Cu-binding protein]]
 [[Category: Mitochondrial assembly factor]]
 [[Category: Redox]]

1wp0

From Proteopedia

Revision as of 12:29, 6 January 2015

Human SCO1

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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