6rsk: Difference between revisions
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==Cytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and 15 eq. spermine - structure II== | |||
<StructureSection load='6rsk' size='340' side='right'caption='[[6rsk]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rsk]] is a 2 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=6RSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RSK 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gd9|6gd9]], [[6gda|6gda]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rsk OCA], [http://pdbe.org/6rsk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rsk RCSB], [http://www.ebi.ac.uk/pdbsum/6rsk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rsk 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 == | |||
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<ref>PMID:31490058</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Crowley, P | <div class="pdbe-citations 6rsk" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Baker's yeast]] | |||
[[Category: Large Structures]] | |||
[[Category: Crowley, P B]] | |||
[[Category: Engilberge, S]] | [[Category: Engilberge, S]] | ||
[[Category: Calixarene]] | |||
[[Category: Molecular glue]] | |||
[[Category: Molecular switch]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Polyamine]] | |||
[[Category: Spermine]] | |||
[[Category: Supramolecular chemistry]] | |||
Revision as of 11:10, 23 October 2019
Cytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and 15 eq. spermine - structure IICytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and 15 eq. spermine - structure II
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 PubMedProtein 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. References
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