7pr3: Difference between revisions
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<StructureSection load='7pr3' size='340' side='right'caption='[[7pr3]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='7pr3' size='340' side='right'caption='[[7pr3]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pr3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pr3]] is a 4 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=7PR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR3 FirstGlance]. <br> | ||
</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7pr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr3 OCA], [https://pdbe.org/7pr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr3 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr3 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=7pr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr3 OCA], [https://pdbe.org/7pr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr3 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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 7pr3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7pr3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Crowley PB]] | ||
[[Category: | [[Category: Flood RJ]] | ||
[[Category: | [[Category: Guagnini F]] | ||
[[Category: | [[Category: Ramberg K]] | ||
Latest revision as of 16:08, 1 February 2024
Cocrystal Form I of a cytochrome c, sulfonato-thiacalix[4]arene - zinc clusterCocrystal Form I of a cytochrome c, sulfonato-thiacalix[4]arene - zinc cluster
Structural highlights
FunctionCYC1_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 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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