2ggt

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(New page: 200px<br /> <applet load="2ggt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ggt, resolution 2.40&Aring;" /> '''Crystal structure o...)
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[[Image:2ggt.gif|left|200px]]<br />
 
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<applet load="2ggt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ggt, resolution 2.40&Aring;" />
 
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'''Crystal structure of human SCO1 complexed with nickel.'''<br />
 
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==Overview==
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==Crystal structure of human SCO1 complexed with nickel.==
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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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<StructureSection load='2ggt' size='340' side='right'caption='[[2ggt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ggt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GGT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ggt OCA], [https://pdbe.org/2ggt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ggt RCSB], [https://www.ebi.ac.uk/pdbsum/2ggt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ggt ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SCO1_HUMAN SCO1_HUMAN] Defects in SCO1 are a cause of mitochondrial complex IV deficiency (MT-C4D) [MIM:[https://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>
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== Function ==
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[https://www.uniprot.org/uniprot/SCO1_HUMAN SCO1_HUMAN] Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX.<ref>PMID:17189203</ref> <ref>PMID:15659396</ref> <ref>PMID:16735468</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/2ggt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ggt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Disease==
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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:16735468<ref>PMID:16735468</ref>
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Known diseases associated with this structure: Hepatic failure, early onset, and neurologic disorder OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603644 603644]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2GGT 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].
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</div>
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<div class="pdbe-citations 2ggt" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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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]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Banci, L.]]
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[[Category: Banci L]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Calderone, V.]]
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[[Category: Calderone V]]
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[[Category: Ciofi-Baffoni, S.]]
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[[Category: Ciofi-Baffoni S]]
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[[Category: Mangani, S.]]
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[[Category: Mangani S]]
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[[Category: Martinelli, M.]]
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[[Category: Martinelli M]]
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[[Category: Palumaa, P.]]
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[[Category: Palumaa P]]
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[[Category: Wang, S.]]
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[[Category: Wang S]]
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[[Category: CL]]
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[[Category: NI]]
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[[Category: copper chaperone]]
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[[Category: cu-binding protein]]
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[[Category: disuplhide]]
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[[Category: mitochondrial assembly factor]]
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[[Category: mitochondrion]]
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[[Category: nickel]]
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[[Category: redox]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:18:34 2007''
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Current revision

Crystal structure of human SCO1 complexed with nickel.

PDB ID 2ggt

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