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| | <StructureSection load='6gda' size='340' side='right'caption='[[6gda]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='6gda' size='340' side='right'caption='[[6gda]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gda]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GDA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gda]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GDA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EVB:sulfonato-calix[8]arene'>EVB</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gd6|6gd6]], [[6gd7|6gd7]], [[6gd8|6gd8]], [[6gd9|6gd9]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYC1, YJR048W, J1653 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6gda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gda OCA], [https://pdbe.org/6gda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gda RCSB], [https://www.ebi.ac.uk/pdbsum/6gda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gda 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=6gda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gda OCA], [http://pdbe.org/6gda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gda RCSB], [http://www.ebi.ac.uk/pdbsum/6gda PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gda ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. | + | [https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Crowley, P B]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Fox, G C]] | + | [[Category: Crowley PB]] |
| - | [[Category: Rennie, M L]] | + | [[Category: Fox GC]] |
| - | [[Category: Assembly]] | + | [[Category: Rennie ML]] |
| - | [[Category: Calixarene]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Scaffold]]
| + | |
| - | [[Category: Supramolecular]]
| + | |
| Structural highlights
Function
CYC1_YEAST Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Publication Abstract from PubMed
Protein crystals with their precise, periodic array of functional building blocks have potential applications in biomaterials, sensing, and catalysis. This paper describes how a highly porous crystalline framework of a cationic redox protein and an anionic macrocycle can be modulated by a small cationic effector. Ternary composites of protein ( approximately 13 kDa), calix[8]arene ( approximately 1.5 kDa), and effector ( approximately 0.2 kDa) formed distinct crystalline architectures, dependent on the effector concentration and the crystallization technique. A combination of X-ray crystallography and density functional theory (DFT) calculations was used to decipher the framework variations, which appear to be dependent on a calixarene conformation change mediated by the effector. This "switch" calixarene was observed in three states, each of which is associated with a different interaction network. Two structures obtained by co-crystallization with the effector contained an additional protein "pillar", resulting in framework duplication and decreased porosity. These results suggest how protein assembly can be engineered by supramolecular host-guest interactions.
Tuning Protein Frameworks via Auxiliary Supramolecular Interactions.,Engilberge S, Rennie ML, Dumont E, Crowley PB ACS Nano. 2019 Sep 24;13(9):10343-10350. doi: 10.1021/acsnano.9b04115. Epub 2019 , Sep 10. PMID:31490058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Engilberge S, Rennie ML, Dumont E, Crowley PB. Tuning Protein Frameworks via Auxiliary Supramolecular Interactions. ACS Nano. 2019 Sep 24;13(9):10343-10350. doi: 10.1021/acsnano.9b04115. Epub 2019 , Sep 10. PMID:31490058 doi:http://dx.doi.org/10.1021/acsnano.9b04115
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