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| | ==Solution structure of Zn(II)Cox4== | | ==Solution structure of Zn(II)Cox4== |
| - | <StructureSection load='2odx' size='340' side='right'caption='[[2odx]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='2odx' size='340' side='right'caption='[[2odx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2odx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2odx]] 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=2ODX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COX4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span></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=2odx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odx OCA], [https://pdbe.org/2odx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odx RCSB], [https://www.ebi.ac.uk/pdbsum/2odx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odx ProSAT]</span></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=2odx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odx OCA], [https://pdbe.org/2odx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odx RCSB], [https://www.ebi.ac.uk/pdbsum/2odx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/COX4_YEAST COX4_YEAST] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Cytochrome-c oxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: III, J H.Coyne]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: All beta-protein]]
| + | [[Category: Coyne III JH]] |
| - | [[Category: Metallo-protein]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
COX4_YEAST
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
Yeast Cox4 is a zinc binding subunit of cytochrome c oxidase. Cox4 is the only cofactor-containing subunit that is not directly part of the catalytic core of the enzyme located in the mitochondrial inner membrane. The Zn(II) site is shown to be distinct from the bovine ortholog, as it results from the x-ray structure of the entire cytochrome c oxidase in having a single histidyl residue and three conserved cysteines residues in the coordination sphere. Substitutions at the Cys ligand positions result in non-functional Cox4 proteins that fail to lead to cytochrome oxidase assembly. Limited function exists in His-119 mutants when overexpressed. Zn(II) binding in Cox4 is, therefore, important for the stability of the complex. The solution structure of yeast Cox4 elucidated by multidimensional NMR reveals a C-terminal globular domain consisting of two beta sheets analogous to the bovine ortholog except the loop containing the coordinating His in the yeast protein and the fourth Cys in the bovine protein are in different positions in the two structures. The conformation of this loop is dictated by the different sequence position of the fourth coordinating zinc ligand. The Zn(II) ion is buried within the domain, consistent with its role in structural stability. Potential functions of this matrix-facing subunit are discussed.
The characterization and role of zinc binding in yeast Cox4.,Coyne HJ 3rd, Ciofi-Baffoni S, Banci L, Bertini I, Zhang L, George GN, Winge DR J Biol Chem. 2007 Mar 23;282(12):8926-34. Epub 2007 Jan 10. PMID:17215247[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coyne HJ 3rd, Ciofi-Baffoni S, Banci L, Bertini I, Zhang L, George GN, Winge DR. The characterization and role of zinc binding in yeast Cox4. J Biol Chem. 2007 Mar 23;282(12):8926-34. Epub 2007 Jan 10. PMID:17215247 doi:10.1074/jbc.M610303200
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