3wc8

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'''Unreleased structure'''
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{{STRUCTURE_3wc8| PDB=3wc8 | SCENE= }}
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===Dimeric horse cytochrome c obtained by refolding with desalting method===
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{{ABSTRACT_PUBMED_24206001}}
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The entry 3wc8 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/CYC_HORSE 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).
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Authors: Parui, P.P., Deshpande, M., Nagao, S., Kamikubo, H., Komori, H., Higuchi, Y., Kataoka, M., Hirota, S.
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==About this Structure==
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[[3wc8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WC8 OCA].
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Description: Dimeric horse cytochrome c obtained by refolding with desalting method
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==Reference==
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<ref group="xtra">PMID:024206001</ref><references group="xtra"/><references/>
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[[Category: Equus caballus]]
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[[Category: Deshpande, M S.]]
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[[Category: Higuchi, Y.]]
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[[Category: Hirota, S.]]
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[[Category: Kamikubo, H.]]
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[[Category: Kataoka, M.]]
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[[Category: Komori, H.]]
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[[Category: Nagao, S.]]
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[[Category: Parui, P P.]]
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[[Category: Electron transport]]

Revision as of 13:33, 11 December 2013

Template:STRUCTURE 3wc8

Contents

Dimeric horse cytochrome c obtained by refolding with desalting method

Template:ABSTRACT PUBMED 24206001

Function

[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).

About this Structure

3wc8 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

  • Parui PP, Deshpande MS, Nagao S, Kamikubo H, Komori H, Higuchi Y, Kataoka M, Hirota S. Formation of Oligomeric Cytochrome c during Folding by Intermolecular Hydrophobic Interaction between N- and C-Terminal alpha-Helices. Biochemistry. 2013 Dec 3;52(48):8732-44. doi: 10.1021/bi400986g. Epub 2013 Nov, 20. PMID:24206001 doi:http://dx.doi.org/10.1021/bi400986g

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