6gd6: Difference between revisions

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==Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with ammonium sulfate==
==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]] 1.20&Aring;' scene=''>
<StructureSection load='6gd6' size='340' side='right'caption='[[6gd6]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6gd6]] 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=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>
<table><tr><td colspan='2'>[[6gd6]] 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=6GD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</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='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></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=6gd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gd6 OCA], [https://pdbe.org/6gd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gd6 RCSB], [https://www.ebi.ac.uk/pdbsum/6gd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gd6 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=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>
</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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</div>
</div>
<div class="pdbe-citations 6gd6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6gd6" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Baker's yeast]]
[[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]]

Latest revision as of 10:58, 17 October 2024

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

6gd6 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rennie M, Fox G, Perez J, Crowley PB. Auto-regulated Protein Assembly on a Supramolecular Scaffold. Angew Chem Int Ed Engl. 2018 Aug 15. doi: 10.1002/anie.201807490. PMID:30109907 doi:http://dx.doi.org/10.1002/anie.201807490

6gd6, resolution 1.20Å

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OCA