4nfg: Difference between revisions
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<StructureSection load='4nfg' size='340' side='right'caption='[[4nfg]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='4nfg' size='340' side='right'caption='[[4nfg]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nfg]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4nfg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NFG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=4nfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfg OCA], [https://pdbe.org/4nfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nfg RCSB], [https://www.ebi.ac.uk/pdbsum/4nfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Bashir Q]] | ||
[[Category: | [[Category: Meulenbroek EM]] | ||
[[Category: | [[Category: Pannu NS]] | ||
[[Category: | [[Category: Ubbink M]] | ||
Latest revision as of 10:13, 27 November 2024
K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complexK13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex
Structural highlights
FunctionCCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMedIt has been demonstrated that the complex of yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP) exists as a delicate equilibrium between a specific, active state and the non-specific, dynamic encounter state. The ortholog of yeast Cc, horse Cc, binds CcP but forms a much more dynamic complex, as demonstrated by NMR spectroscopy. A single conservative mutation of lysine 13 to arginine reduces the dynamics and enhances the specificity. The crystal structure of the stereospecific complex resembles the yeast Cc-CcP complex. In contrast, the K13A mutation increases the dynamic nature of the complex with CcP, showing that specificity in a redox protein complex can depend on the interactions of a single side chain in the binding interface. This article is protected by copyright. All rights reserved. STRUCTURED DIGITAL ABSTRACT: hCc and yCcP bind by nuclear magnetic resonance (1, 2, 3) hCc and yCcP bind by x-ray crystallography (View interaction). Engineering specificity in a dynamic protein complex with a single conserved mutation.,Bashir Q, Meulenbroek EM, Pannu NS, Ubbink M FEBS J. 2014 Sep 2. doi: 10.1111/febs.13028. PMID:25180929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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