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| | ==Solution nmr structure of a yeast iso-1-ferrocytochrome C== | | ==Solution nmr structure of a yeast iso-1-ferrocytochrome C== |
| - | <StructureSection load='1yfc' size='340' side='right'caption='[[1yfc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1yfc' size='340' side='right'caption='[[1yfc]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yfc]] is a 1 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=1YFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yfc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFC FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></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=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YEAST ISO-1-CYTOCHROME C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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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=1yfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfc OCA], [https://pdbe.org/1yfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfc RCSB], [https://www.ebi.ac.uk/pdbsum/1yfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfc ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfc OCA], [https://pdbe.org/1yfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfc RCSB], [https://www.ebi.ac.uk/pdbsum/1yfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baistrocchi, P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Banci, L]] | + | [[Category: Baistrocchi P]] |
| - | [[Category: Bertini, I]] | + | [[Category: Banci L]] |
| - | [[Category: Bren, K L]] | + | [[Category: Bertini I]] |
| - | [[Category: Gray, H B]] | + | [[Category: Bren KL]] |
| - | [[Category: Turano, P]] | + | [[Category: Gray HB]] |
| - | [[Category: Electron transport]]
| + | [[Category: Turano P]] |
| - | [[Category: Ferrocytochrome]]
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| - | [[Category: Methylation]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Respiratory chain]]
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| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two-dimensional 1H NMR spectra of Saccharomyces cerevisiae reduced iso-1-cytochrome c have been used to confirm and slightly extend the assignment available in the literature. 1702 NOESY cross-peaks have been assigned, and their intensities have been measured. Through the program DIANA and related protocols (Guntert, 1992), a solution structure has been obtained by using 1442 meaningful NOEs and 13 hydrogen-bond constraints. The RMSD values with respect to the mean structure for the backbone and all heavy atoms for a family of 20 structures are 0.61 +/- 0.09 and 0.98 +/- 0.09 A, the average target function value being as small as 0.57 A2. The larger number of slowly exchanging amide NHs observed in this system compared to that observed in the cyanide derivative of oxidized Ala 80 cytochrome c suggests that the oxidized form is much more flexible and that the backbone protons are more solvent accessible. Comparison of the present structure with the crystal structures of reduced yeast cytochrome c and of the complex between cytochrome c peroxidase and oxidized yeast cytochrome c reveals substantial similarity among the backbone conformations but differences in the residues located in the region of protein-protein interaction. Interestingly, in solution the peripheral residues involved in the interaction with cytochrome c peroxidase are on average closer to the position found in the crystal structure of the complex than to the solid state structure of the isolated reduced from.
Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c.,Baistrocchi P, Banci L, Bertini I, Turano P, Bren KL, Gray HB Biochemistry. 1996 Oct 29;35(43):13788-96. PMID:8901521[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baistrocchi P, Banci L, Bertini I, Turano P, Bren KL, Gray HB. Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c. Biochemistry. 1996 Oct 29;35(43):13788-96. PMID:8901521 doi:10.1021/bi961110e
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