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4nfg

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Revision as of 08:56, 10 April 2019

K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

Structural highlights

4nfg is a 2 chain structure with sequence from Atcc 18824 and Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	CCP1, CCP, CPO, YKR066C (ATCC 18824), CYCS, CYC (Equus caballus)
Activity:	Cytochrome-c peroxidase, with EC number 1.11.1.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [CYC_HORSE] 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. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bashir Q, Meulenbroek EM, Pannu NS, Ubbink M. Engineering specificity in a dynamic protein complex with a single conserved mutation. FEBS J. 2014 Sep 2. doi: 10.1111/febs.13028. PMID:25180929 doi:http://dx.doi.org/10.1111/febs.13028

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nfg"

@@ Line 1: / Line 1: @@
 ==K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex==
-<StructureSection load='4nfg' size='340' side='right' caption='[[4nfg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
+<StructureSection load='4nfg' size='340' side='right'caption='[[4nfg]], [[Resolution|resolution]] 2.11&Aring;' 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>
+<table><tr><td colspan='2'>[[4nfg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. 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 id='ligand'><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></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP1, CCP, CPO, YKR066C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CYCS, CYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr>
 <tr id='activity'><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 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=4nfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfg OCA], [http://pdbe.org/4nfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nfg RCSB], [http://www.ebi.ac.uk/pdbsum/4nfg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfg ProSAT]</span></td></tr>
@@ Line 26: / Line 27: @@
 __TOC__
 </StructureSection>
+[[Category: Atcc 18824]]
 [[Category: Cytochrome-c peroxidase]]
+[[Category: Equus caballus]]
+[[Category: Large Structures]]
 [[Category: Bashir, Q]]
 [[Category: Meulenbroek, E M]]

4nfg

From Proteopedia

Revision as of 08:56, 10 April 2019

K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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