|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==NMR Solution Structure of Yeast Iso-1-cytochrome c Mutant P71H in reduced states== | | ==NMR Solution Structure of Yeast Iso-1-cytochrome c Mutant P71H in reduced states== |
| - | <StructureSection load='2lit' size='340' side='right' caption='[[2lit]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lit' size='340' side='right'caption='[[2lit]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lit]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LIT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LIT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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, 20 models</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lir|2lir]]</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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYC1, YJR048W, J1653 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=2lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lit OCA], [https://pdbe.org/2lit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lit RCSB], [https://www.ebi.ac.uk/pdbsum/2lit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lit ProSAT]</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=2lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lit OCA], [http://pdbe.org/2lit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lit RCSB], [http://www.ebi.ac.uk/pdbsum/2lit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lit ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Cytochrome c|Cytochrome c]] | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Cao, C]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Huang, Z X]] | + | [[Category: Cao C]] |
| - | [[Category: Jiang, X]] | + | [[Category: Huang ZX]] |
| - | [[Category: Lan, W]] | + | [[Category: Jiang X]] |
| - | [[Category: Liu, M]] | + | [[Category: Lan W]] |
| - | [[Category: Tan, X]] | + | [[Category: Liu M]] |
| - | [[Category: Wang, Z]] | + | [[Category: Tan X]] |
| - | [[Category: Wu, H]] | + | [[Category: Wang Z]] |
| - | [[Category: Yang, Z]] | + | [[Category: Wu H]] |
| - | [[Category: Ying, T]] | + | [[Category: Yang Z]] |
| - | [[Category: Zhang, X]] | + | [[Category: Ying T]] |
| - | [[Category: Zhu, J]] | + | [[Category: Zhang X]] |
| - | [[Category: Cytochrome c]]
| + | [[Category: Zhu J]] |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: P71h]]
| + | |
| - | [[Category: Reduced]]
| + | |
| 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.
Publication Abstract from PubMed
To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.
Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced States.,Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX PLoS One. 2011;6(11):e27219. Epub 2011 Nov 8. PMID:22087268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX. Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced States. PLoS One. 2011;6(11):e27219. Epub 2011 Nov 8. PMID:22087268 doi:10.1371/journal.pone.0027219
|
