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.
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| 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.
See Also
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
