7pr4: Difference between revisions
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==Cocrystal Form II of a cytochrome c, sulfonato-thiacalix[4]arene - zinc cluster== | ==Cocrystal Form II of a cytochrome c, sulfonato-thiacalix[4]arene - zinc cluster== | ||
<StructureSection load='7pr4' size='340' side='right'caption='[[7pr4]]' scene=''> | <StructureSection load='7pr4' size='340' side='right'caption='[[7pr4]], [[Resolution|resolution]] 1.32Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pr4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PR4 FirstGlance]. <br> | ||
</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=7pr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr4 OCA], [https://pdbe.org/7pr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr4 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr4 ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7pr2|7pr2]], [[7pr3|7pr3]]</div></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=7pr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pr4 OCA], [https://pdbe.org/7pr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pr4 RCSB], [https://www.ebi.ac.uk/pdbsum/7pr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pr4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7pr4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Crowley | [[Category: Crowley, P B]] | ||
[[Category: Flood | [[Category: Flood, R J]] | ||
[[Category: Guagnini F]] | [[Category: Guagnini, F]] | ||
[[Category: Ramberg K]] | [[Category: Ramberg, K]] | ||
[[Category: Alpha helix]] | |||
[[Category: Calixarene]] | |||
[[Category: Electron transport]] | |||
[[Category: Metal cluster]] | |||
[[Category: Molecular glue]] | |||
[[Category: Synthetic receptor]] | |||
[[Category: Thiacalixarene]] | |||
Revision as of 13:23, 18 May 2022
Cocrystal Form II of a cytochrome c, sulfonato-thiacalix[4]arene - zinc clusterCocrystal Form II of a cytochrome c, sulfonato-thiacalix[4]arene - zinc cluster
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 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. References
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