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| | ==Crystal Structure of Yeast Sco1 with Copper Bound== | | ==Crystal Structure of Yeast Sco1 with Copper Bound== |
| - | <StructureSection load='2b7j' size='340' side='right' caption='[[2b7j]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2b7j' size='340' side='right'caption='[[2b7j]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b7j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b7j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B7J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b7k|2b7k]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2b7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7j OCA], [https://pdbe.org/2b7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b7j RCSB], [https://www.ebi.ac.uk/pdbsum/2b7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7j ProSAT]</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=2b7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7j OCA], [http://pdbe.org/2b7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b7j RCSB], [http://www.ebi.ac.uk/pdbsum/2b7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCO1_YEAST SCO1_YEAST]] Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.<ref>PMID:16570183</ref> | + | [https://www.uniprot.org/uniprot/SCO1_YEAST SCO1_YEAST] Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.<ref>PMID:16570183</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/2b7j_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/2b7j_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Abajian, C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Rosenzweig, A C]] | + | [[Category: Abajian C]] |
| - | [[Category: Cytochrome c oxidase]] | + | [[Category: Rosenzweig AC]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metallochaperone]]
| + | |
| - | [[Category: Sco]]
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| - | [[Category: Sco1]]
| + | |
| Structural highlights
Function
SCO1_YEAST Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.[1]
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
The Sco family of proteins are involved in the assembly of the dinuclear CuA site in cytochrome c oxidase (COX), the terminal enzyme in aerobic respiration. These proteins, which are found in both eukaryotes and prokaryotes, are characterized by a conserved CXXXC sequence motif that binds copper ions and that has also been proposed to perform a thiol:disulfide oxidoreductase function. The crystal structures of Saccharomyces cerevisiae apo Sco1 (apo-ySco1) and Sco1 in the presence of copper ions (Cu-ySco1) were determined to 1.8- and 2.3-A resolutions, respectively. Yeast Sco1 exhibits a thioredoxin-like fold, similar to that observed for human Sco1 and a homolog from Bacillus subtilis. The Cu-ySco1 structure, obtained by soaking apo-ySco1 crystals in copper ions, reveals an unexpected copper-binding site involving Cys181 and Cys216, cysteine residues present in ySco1 but not in other homologs. The conserved CXXXC cysteines, Cys148 and Cys152, can undergo redox chemistry in the crystal. An essential histidine residue, His239, is located on a highly flexible loop, denoted the Sco loop, and can adopt positions proximal to both pairs of cysteines. Interactions between ySco1 and its partner proteins yeast Cox17 and yeast COX2 are likely to occur via complementary electrostatic surfaces. This high-resolution model of a eukaryotic Sco protein provides new insight into Sco copper binding and function.
Crystal structure of yeast Sco1.,Abajian C, Rosenzweig AC J Biol Inorg Chem. 2006 Jun;11(4):459-66. Epub 2006 Mar 29. PMID:16570183[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abajian C, Rosenzweig AC. Crystal structure of yeast Sco1. J Biol Inorg Chem. 2006 Jun;11(4):459-66. Epub 2006 Mar 29. PMID:16570183 doi:http://dx.doi.org/10.1007/s00775-006-0096-7
- ↑ Abajian C, Rosenzweig AC. Crystal structure of yeast Sco1. J Biol Inorg Chem. 2006 Jun;11(4):459-66. Epub 2006 Mar 29. PMID:16570183 doi:http://dx.doi.org/10.1007/s00775-006-0096-7
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