6gd6: Difference between revisions
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==Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with ammonium sulfate== | |||
<StructureSection load='6gd6' size='340' side='right' caption='[[6gd6]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gd6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GD6 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></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gd7|6gd7]], [[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=6gd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gd6 OCA], [http://pdbe.org/6gd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gd6 RCSB], [http://www.ebi.ac.uk/pdbsum/6gd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gd6 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 6gd6" 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 10:33, 29 August 2018
Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with ammonium sulfateCytochrome c in complex with Sulfonato-calix[8]arene, H3 form with ammonium sulfate
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 PubMedControlled 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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