4nfg: Difference between revisions
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''' | ==K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex== | ||
<StructureSection load='4nfg' size='340' side='right' caption='[[4nfg]], [[Resolution|resolution]] 2.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nfg]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nfg RCSB], [http://www.ebi.ac.uk/pdbsum/4nfg PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
It 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<ref>PMID:25180929</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cytochrome-c peroxidase]] | |||
[[Category: Bashir, Q.]] | |||
[[Category: Meulenbroek, E M.]] | |||
[[Category: Pannu, N S.]] | |||
[[Category: Ubbink, M.]] | |||
[[Category: Oxidoreductase-electron transport complex]] | |||
[[Category: Oxidoreductase/electron transport]] | |||
Revision as of 10:30, 24 September 2014
K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex
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