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7mri
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N63T yeast iso-1-cytochrome c== | |
| + | <StructureSection load='7mri' size='340' side='right'caption='[[7mri]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7mri]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MRI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.46Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7mri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mri OCA], [https://pdbe.org/7mri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mri RCSB], [https://www.ebi.ac.uk/pdbsum/7mri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mri ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Naturally-occurring variants of human cytochrome c (Cytc) that induce thrombocytopenia IV occur within Omega-loop C (residues 40-57). These variants enhance the peroxidase activity of human Cytc apparently by facilitating access to the heme by destabilizing Omega-loops C and D (residues 70-85). Given the importance of peroxidase activity in the early stages of apoptosis, we identified three sites with the EVmutation algorithm in or near Omega-loop C that coevolve and differ between yeast iso-1-Cytc and human Cytc. We prepared iso-1-Cytc variants with all possible combinations of the S40T, V57I and N63T substitutions to determine if these residues decrease the peroxidase activity of iso-1-Cytc to that of human Cytc producing an effective off state for a peroxidase signaling switch. At pH 6 and above, all variants significantly decreased peroxidase activity. However, the correlation of peroxidase activity with local and global stability, expected if cooperative unfolding of Omega-loops C and D is required for peroxidase activity, was generally poor. The m-values derived from the guanidine hydrochloride dependence of the kinetics of imidazole binding to horse Cytc, which is well-characterized by native-state hydrogen exchange methods, and K72A/K73A/K79A iso-1-Cytc show that local structural fluctuations and not subglobal cooperative unfolding of Omega-loops C and D are sufficient to permit binding of a small molecule like peroxide to the heme. A 2.46 A structure of N63T iso-1-Cytc identifies a change to a hydrogen bond network linking Omega-loops C and D that could modulate the local fluctuations needed for the intrinsic peroxidase activity of Cytc. | ||
| - | + | Effect on intrinsic peroxidase activity of substituting coevolved residues from Omega-loop C of human cytochrome c into yeast iso-1-cytochrome c.,Frederick AK, Thompson SL, Vakharia ZM, Cherney MM, Lei H, Evenson G, Bowler BE J Inorg Biochem. 2022 Jul;232:111819. doi: 10.1016/j.jinorgbio.2022.111819. Epub , 2022 Apr 6. PMID:35428021<ref>PMID:35428021</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7mri" style="background-color:#fffaf0;"></div> |
| - | [[Category: Bowler | + | |
| - | [[Category: Lei | + | ==See Also== |
| + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Bowler BE]] | ||
| + | [[Category: Evenson GE]] | ||
| + | [[Category: Lei H]] | ||
Current revision
Crystal structure of N63T yeast iso-1-cytochrome c
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