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2gb8

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[[Image:2gb8.gif|left|200px]]
 
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{{Structure
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==Solution structure of the complex between yeast iso-1-cytochrome c and yeast cytochrome c peroxidase==
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|PDB= 2gb8 |SIZE=350|CAPTION= <scene name='initialview01'>2gb8</scene>
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<StructureSection load='2gb8' size='340' side='right'caption='[[2gb8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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<table><tr><td colspan='2'>[[2gb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GB8 FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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|GENE= CCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), CYC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pcc|2pcc]], [[1s6v|1s6v]], [[1zby|1zby]], [[1ycc|1ycc]]</div></td></tr>
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|DOMAIN=
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CYC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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|RELATEDENTRY=[[2pcc|2PCC]], [[1s6v|1S6V]], [[1zby|1ZBY]], [[1ycc|1YCC]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb8 OCA], [http://www.ebi.ac.uk/pdbsum/2gb8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gb8 RCSB]</span>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb8 OCA], [https://pdbe.org/2gb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gb8 RCSB], [https://www.ebi.ac.uk/pdbsum/2gb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb8 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/2gb8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gb8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The physiological complex of yeast cytochrome c peroxidase and iso-1-cytochrome c is a paradigm for biological electron transfer. Using paramagnetic NMR spectroscopy, we have determined the conformation of the protein complex in solution, which is shown to be very similar to that observed in the crystal structure [Pelletier H, Kraut J (1992) Science 258:1748-1755]. Our results support the view that this transient electron transfer complex is dynamic. The solution structure represents the dominant protein-protein orientation, which, according to our estimates, is occupied for &gt;70% of the lifetime of the complex, with the rest of the time spent in the dynamic encounter state. Based on the observed paramagnetic effects, we have delineated the conformational space sampled by the protein molecules during the dynamic part of the interaction, providing experimental support for the theoretical predictions of the classical Brownian dynamics study [Northrup SH, Boles JO, Reynolds JCL (1988) Science 241:67-70]. Our findings corroborate the dynamic behavior of this complex and offer an insight into the mechanism of the protein complex formation in solution.
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'''Solution structure of the complex between yeast iso-1-cytochrome c and yeast cytochrome c peroxidase'''
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Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR.,Volkov AN, Worrall JA, Holtzmann E, Ubbink M Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18945-50. Epub 2006 Dec 4. PMID:17146057<ref>PMID:17146057</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2gb8" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The physiological complex of yeast cytochrome c peroxidase and iso-1-cytochrome c is a paradigm for biological electron transfer. Using paramagnetic NMR spectroscopy, we have determined the conformation of the protein complex in solution, which is shown to be very similar to that observed in the crystal structure [Pelletier H, Kraut J (1992) Science 258:1748-1755]. Our results support the view that this transient electron transfer complex is dynamic. The solution structure represents the dominant protein-protein orientation, which, according to our estimates, is occupied for &gt;70% of the lifetime of the complex, with the rest of the time spent in the dynamic encounter state. Based on the observed paramagnetic effects, we have delineated the conformational space sampled by the protein molecules during the dynamic part of the interaction, providing experimental support for the theoretical predictions of the classical Brownian dynamics study [Northrup SH, Boles JO, Reynolds JCL (1988) Science 241:67-70]. Our findings corroborate the dynamic behavior of this complex and offer an insight into the mechanism of the protein complex formation in solution.
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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==About this Structure==
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== References ==
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2GB8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB8 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR., Volkov AN, Worrall JA, Holtzmann E, Ubbink M, Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18945-50. Epub 2006 Dec 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17146057 17146057]
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[[Category: Atcc 18824]]
[[Category: Cytochrome-c peroxidase]]
[[Category: Cytochrome-c peroxidase]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Ubbink, M]]
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[[Category: Ubbink, M.]]
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[[Category: Volkov, A N]]
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[[Category: Volkov, A N.]]
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[[Category: Worrall, J A.R]]
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[[Category: Worrall, J A.R.]]
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[[Category: Electron transfer]]
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[[Category: electron transfer]]
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[[Category: Oxidoreductase-electron transport complex]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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[[Category: transient complex]]
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[[Category: Transient complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:14:17 2008''
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Current revision

Solution structure of the complex between yeast iso-1-cytochrome c and yeast cytochrome c peroxidase

PDB ID 2gb8

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