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| | <StructureSection load='1lfm' size='340' side='right'caption='[[1lfm]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1lfm' size='340' side='right'caption='[[1lfm]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lfm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LFM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lfm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LFM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COH:PROTOPORPHYRIN+IX+CONTAINING+CO'>COH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i54|1i54]], [[1i55|1i55]], [[3cyt|3cyt]], [[5cyt|5cyt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COH:PROTOPORPHYRIN+IX+CONTAINING+CO'>COH</scene></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=1lfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfm OCA], [http://pdbe.org/1lfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lfm RCSB], [http://www.ebi.ac.uk/pdbsum/1lfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfm 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=1lfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfm OCA], [https://pdbe.org/1lfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lfm RCSB], [https://www.ebi.ac.uk/pdbsum/1lfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYC_THUAA CYC_THUAA]] 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/CYC_THUAA CYC_THUAA] 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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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Thunnus thynnus]] | | [[Category: Thunnus thynnus]] |
| - | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
| - | [[Category: Findley, W M]] | + | [[Category: Findley WM]] |
| - | [[Category: Gray, H B]] | + | [[Category: Gray HB]] |
| - | [[Category: Lyubovitsky, J G]] | + | [[Category: Lyubovitsky JG]] |
| - | [[Category: Ross, S A]] | + | [[Category: Ross SA]] |
| - | [[Category: Tezcan, F A]] | + | [[Category: Tezcan FA]] |
| - | [[Category: Winkler, J R]] | + | [[Category: Winkler JR]] |
| - | [[Category: Cytochrome c]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Folding]]
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| - | [[Category: Intermediate]]
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| Structural highlights
Function
CYC_THUAA 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
Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Remarkably, neither the protein structure nor the folding thermodynamics is perturbed by this metal-ion substitution, as shown by data from spectroscopic and x-ray diffraction experiments. Through kinetics measurements, we have found parallel folding pathways involving several different misligated Co(III) species, and, as these folding intermediates persist for several hours under certain conditions, we have been able to elucidate fully their spectroscopic properties. The results, along with an analysis of the fluorescence energy-transfer kinetics during refolding, show that rapidly equilibrating populations of compact and extended polypeptide conformations are present until all molecules have reached the native structure. These measurements provide direct evidence that collapsed denatured structures are not substantially more stable than extended conformations of cytochrome c.
Using deeply trapped intermediates to map the cytochrome c folding landscape.,Tezcan FA, Findley WM, Crane BR, Ross SA, Lyubovitsky JG, Gray HB, Winkler JR Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8626-30. PMID:12084923[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tezcan FA, Findley WM, Crane BR, Ross SA, Lyubovitsky JG, Gray HB, Winkler JR. Using deeply trapped intermediates to map the cytochrome c folding landscape. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8626-30. PMID:12084923 doi:10.1073/pnas.132254499
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