5lyc: Difference between revisions

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-'''Unreleased structure'''
-The entry 5lyc is ON HOLD
+==Cytochrome c in complex with phosphonato-calix[6]arene==
+<StructureSection load='5lyc' size='340' side='right' caption='[[5lyc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5lyc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LYC FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7AZ:PHOSPHONATO-CALIX[6]ARENE'>7AZ</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5lyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lyc OCA], [http://pdbe.org/5lyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lyc RCSB], [http://www.ebi.ac.uk/pdbsum/5lyc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lyc 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 ==
+Complex formation between cationic cytochrome c and the water-soluble, poly-anionic p-phosphonatocalix[6]arene (pclx6 ) was investigated. A crystal structure (at 1.8 A resolution) revealed a remarkable dimeric disc of pclx6 that acts like glue to mediate a symmetric (C2 ) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 A2 of protein surface. The key protein-calixarene contacts occur via two linchpin lysines, with additional contacts provided by a small hydrophobic patch. The protein-calixarene supramolecular assemblies were observed in solution by size-exclusion chromatography with multi-angle light scattering and NMR spectroscopy. Using isothermal titration calorimetry and NMR data, an apparent Kd in the low micromolar range was determined for the charge-rich protein-calixarene complex. In contrast to p-sulfonatocalix[4]arene, the larger pclx6 has a single, well-defined binding site that mediates the assembly of cytochrome c in solution.
-Authors: Rennie, M.L., Crowley, P.B.
+Protein Dimerization on a Phosphonated Calix[6]arene Disc.,Rennie ML, Doolan AM, Raston CL, Crowley PB Angew Chem Int Ed Engl. 2017 May 8;56(20):5517-5521. doi: 10.1002/anie.201701500., Epub 2017 Apr 13. PMID:28407337<ref>PMID:28407337</ref>
-Description: Cytochrome c in complex with phosphonato-calix[6]arene
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Crowley, P.B]]
+<div class="pdbe-citations 5lyc" style="background-color:#fffaf0;"></div>
-[[Category: Rennie, M.L]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Crowley, P B]]
+[[Category: Rennie, M L]]
+[[Category: Calixarene]]
+[[Category: Dimer]]
+[[Category: Oxidoreductase]]
+[[Category: Surface-binding]]