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1z2g
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1z2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z2g" /> '''Solution structure of apo, oxidized yeast Co...) |
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| - | [[Image:1z2g.gif|left|200px]]<br /><applet load="1z2g" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1z2g" /> | ||
| - | '''Solution structure of apo, oxidized yeast Cox17'''<br /> | ||
| - | == | + | ==Solution structure of apo, oxidized yeast Cox17== |
| - | Cox17 is a key mitochondrial copper chaperone involved in the assembly of | + | <StructureSection load='1z2g' size='340' side='right'caption='[[1z2g]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1z2g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2G FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2g OCA], [https://pdbe.org/1z2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z2g RCSB], [https://www.ebi.ac.uk/pdbsum/1z2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COX17_YEAST COX17_YEAST] Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/1z2g_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1z2g ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cox17 is a key mitochondrial copper chaperone involved in the assembly of cytochrome c oxidase (COX). The NMR solution structure of the oxidized apoCox17 isoform consists of a coiled-coil conformation stabilized by two disulfide bonds involving Cys(26)/Cys(57) and Cys(36)/Cys(47). This appears to be a conserved tertiary fold of a class of proteins, localized within the mitochondrial intermembrane space, that contain a twin Cys-x(9)-Cys sequence motif. An isomerization of one disulfide bond from Cys(26)/Cys(57) to Cys(24)/Cys(57) is required prior to Cu(I) binding to form the Cu(1)Cox17 complex. Upon further oxidation of the apo-protein, a form with three disulfide bonds is obtained. The reduction of all disulfide bonds provides a molten globule form that can convert to an additional conformer capable of binding up to four Cu(I) ions in a polycopper cluster. This form of the protein is oligomeric. These properties are framed within a complete model of mitochondrial import and COX assembly. | ||
| - | + | Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding.,Arnesano F, Balatri E, Banci L, Bertini I, Winge DR Structure. 2005 May;13(5):713-22. PMID:15893662<ref>PMID:15893662</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1z2g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | + | [[Category: Arnesano F]] | |
| - | [[Category: Arnesano | + | [[Category: Balatri E]] |
| - | [[Category: Balatri | + | [[Category: Banci L]] |
| - | [[Category: Banci | + | [[Category: Bertini I]] |
| - | [[Category: Bertini | + | [[Category: Winge DR]] |
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| - | [[Category: Winge | + | |
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Current revision
Solution structure of apo, oxidized yeast Cox17
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