2n18: Difference between revisions
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{{Large structure}} | |||
==Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase== | ==Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase== | ||
<StructureSection load='2n18' size='340' side='right' caption='[[2n18]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2n18' size='340' side='right' caption='[[2n18]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s6v|1s6v]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s6v|1s6v]]</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='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=2n18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2n18 RCSB], [http://www.ebi.ac.uk/pdbsum/2n18 PDBsum]</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=2n18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n18 OCA], [http://pdbe.org/2n18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n18 RCSB], [http://www.ebi.ac.uk/pdbsum/2n18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n18 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | |||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [[http://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] 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. | [[http://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [[http://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] 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. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2n18" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:31, 9 March 2017
Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidaseDominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Function[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [CYC1_YEAST] 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. Publication Abstract from PubMedThe complex of yeast cytochrome c peroxidase and cytochrome c is a paradigm of the biological electron transfer (ET). Building on seven decades of research, two different models have been proposed to explain its functional redox activity. One postulates that the intermolecular ET occurs only in the dominant, high-affinity protein-protein orientation, while the other posits formation of an additional, low-affinity complex, which is much more active than the dominant one. Unlike the high-affinity interaction-extensively studied by X-ray crystallography and NMR spectroscopy-until now the binding of cytochrome c to the low-affinity site has not been observed directly, but inferred mainly from kinetics experiments. Here we report the structure of this elusive, weak protein complex and show that it consists of a dominant, inactive bound species and an ensemble of minor, ET-competent protein-protein orientations, which summarily account for the experimentally determined value of the ET rate constant. The low-affinity complex of cytochrome c and its peroxidase.,Van de Water K, Sterckx YG, Volkov AN Nat Commun. 2015 May 6;6:7073. doi: 10.1038/ncomms8073. PMID:25944250[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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