6gd7
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with PEG== | |
| + | <StructureSection load='6gd7' size='340' side='right' caption='[[6gd7]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gd7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GD7 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gd6|6gd6]], [[6gd8|6gd8]], [[6gd9|6gd9]], [[6gda|6gda]]</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=6gd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gd7 OCA], [http://pdbe.org/6gd7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gd7 RCSB], [http://www.ebi.ac.uk/pdbsum/6gd7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gd7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Controlled protein assembly provides a means to regulate function. Supramolecular building blocks, including rigid macrocycles, have proven to be versatile triggers of protein assembly. Here, we show that sulfonato-calix[8]arene (sclx8) mediates the formation of cytochrome c tetramers in solution. This tetramer spontaneously disassembles at >/= 2 equivalents of sclx8 providing a remarkable example of "auto-regulation". Using X-ray crystallography we characterize in detail the sclx8 binding sites on cytochrome c. Crystal structures at different protein-ligand ratios reveal varying degrees (up to ~35 %) of protein surface coverage by the calixarene and suggest a mechanism for oligomer disassembly. The solution structure of the oligomer was characterized by small angle X-ray scattering. Overall, the data indicate calixarene-controlled protein assembly and disassembly without the requirement for a competitive inhibitor, and point to protein encapsulation by a flexible macrocycle. | ||
| - | + | Auto-regulated Protein Assembly on a Supramolecular Scaffold.,Rennie M, Fox G, Perez J, Crowley PB Angew Chem Int Ed Engl. 2018 Aug 15. doi: 10.1002/anie.201807490. PMID:30109907<ref>PMID:30109907</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6gd7" style="background-color:#fffaf0;"></div> |
| - | [[Category: Rennie, M | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Crowley, P B]] | ||
| + | [[Category: Fox, G C]] | ||
| + | [[Category: Rennie, M L]] | ||
| + | [[Category: Assembly]] | ||
| + | [[Category: Calixarene]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Scaffold]] | ||
| + | [[Category: Supramolecular]] | ||
Revision as of 07:33, 29 August 2018
Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with PEG
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