7pr2

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Current revision (09:05, 17 October 2024) (edit) (undo)
 
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<StructureSection load='7pr2' size='340' side='right'caption='[[7pr2]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
<StructureSection load='7pr2' size='340' side='right'caption='[[7pr2]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7pr2]] is a 2 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=7PR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR2 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</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]] 1.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=80M:sulfonato-thiacalix[4]arene'>80M</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=80M:sulfonato-thiacalix[4]arene'>80M</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></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=7pr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr2 OCA], [https://pdbe.org/7pr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr2 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr2 ProSAT]</span></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=7pr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr2 OCA], [https://pdbe.org/7pr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr2 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr2 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[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.
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Controlled protein assembly provides a means to generate biomaterials. Synthetic macrocycles such as the water-soluble sulfonato-calix[n]arenes are useful mediators of protein assembly. Sulfonato-thiacalix[4]arene (tsclx 4 ), with its metal-binding capacity, affords the potential for simultaneous macrocycle- and metal-mediated protein assembly. Here, we describe the tsclx 4 -/Zn-directed assembly of two proteins: cationic alpha-helical cytochrome c (cyt c) and neutral beta-propeller Ralstonia solanacearum lectin (RSL). Two co-crystal forms were obtained with cyt c, each involving multinuclear zinc sites supported by the cone conformation of tsclx 4 . The tsclx 4 /Zn cluster acted as an assembly node via both lysine encapsulation and metal-mediated protein-protein contacts. In the case of RSL, tsclx 4 adopted the 1,2-alternate conformation and supported a dinuclear zinc site with concomitant encapsulation and metal-binding of two histidine side chains. These results, together with the knowledge of thiacalixarene/metal nanoclusters, suggest promising applications for thiacalixarenes in biomaterials and MOF fabrication.
 
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Protein Frameworks with Thiacalixarene and Zinc.,Flood RJ, Ramberg KO, Mengel DB, Guagnini F, Crowley PB Cryst Growth Des. 2022 May 4;22(5):3271-3276. doi: 10.1021/acs.cgd.2c00108. Epub , 2022 Feb 22. PMID:35529063<ref>PMID:35529063</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7pr2" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
 
[[Category: Crowley PB]]
[[Category: Crowley PB]]
[[Category: Flood RJ]]
[[Category: Flood RJ]]
[[Category: Guagnini F]]
[[Category: Guagnini F]]
[[Category: Ramberg K]]
[[Category: Ramberg K]]

Current revision

Cocrystal of cytochrome c and sulfonato-thiacalix[4]arene

PDB ID 7pr2

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