2ggt

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{{Seed}}
 
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[[Image:2ggt.png|left|200px]]
 
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==Crystal structure of human SCO1 complexed with nickel.==
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The line below this paragraph, containing "STRUCTURE_2ggt", creates the "Structure Box" on the page.
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<StructureSection load='2ggt' size='340' side='right'caption='[[2ggt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_2ggt| PDB=2ggt | SCENE= }}
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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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===Crystal structure of human SCO1 complexed with nickel.===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16735468}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2ggt" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16735468 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16735468}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease 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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2GGT is a [[Single protein]] structure of 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=2GGT OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16735468 16735468]
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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://www.ncbi.nlm.nih.gov/pubmed/15659396 15659396]
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Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly., Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Structure. 2003 Nov;11(11):1431-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14604533 14604533]
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[[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: 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://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:30:26 2008''
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Current revision

Crystal structure of human SCO1 complexed with nickel.

PDB ID 2ggt

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OCA

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