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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2yk3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w9k 2w9k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YK3 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2yk3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w9k 2w9k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YK3 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.55Å</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2yk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yk3 OCA], [https://pdbe.org/2yk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yk3 RCSB], [https://www.ebi.ac.uk/pdbsum/2yk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yk3 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=2yk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yk3 OCA], [https://pdbe.org/2yk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yk3 RCSB], [https://www.ebi.ac.uk/pdbsum/2yk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yk3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CYC_CRIFA CYC_CRIFA]] 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_CRIFA CYC_CRIFA] 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 == |
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| | [[Category: Crithidia fasciculata]] | | [[Category: Crithidia fasciculata]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allen, J W.A]] | + | [[Category: Allen JWA]] |
| - | [[Category: Ferguson, S J]] | + | [[Category: Ferguson SJ]] |
| - | [[Category: Fulop, V]] | + | [[Category: Fulop V]] |
| - | [[Category: Ginger, M L]] | + | [[Category: Ginger ML]] |
| - | [[Category: Sam, K A]] | + | [[Category: Sam KA]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Intermembrane space]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Respiratory chain]]
| + | |
| - | [[Category: Thioether bond]]
| + | |
| - | [[Category: Trypanosome]]
| + | |
| Structural highlights
Function
CYC_CRIFA 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
The principal physiological role of mitochondrial cytochrome c is electron transfer during oxidative phosphorylation. c-Type cytochromes are almost always characterized by covalent attachment of heme to protein through two thioether bonds between the heme vinyl groups and the thiols of cysteine residues in a Cys-Xxx-Xxx-Cys-His motif. Uniquely, however, members of the evolutionarily divergent protist phylum Euglenozoa, which includes Trypanosoma and Leishmania species, have mitochondrial cytochromes c with heme attached through only one thioether bond [to an (A/F)XXCH motif]; the implications of this for the cytochrome structures are unclear. Here we present the 1.55 A resolution X-ray crystal structure of cytochrome c from the trypanosomatid Crithidia fasciculata. Despite the fundamental difference in heme attachment and in the cytochrome c biogenesis machinery of the Euglenozoa, the structure is remarkably similar to that of typical (CXXCH) mitochondrial cytochromes c, both in overall fold and, other than the missing thioether bond, in the details of the heme attachment. Notably, this similarity includes the stereochemistry of the covalent heme attachment to the protein. The structure has implications for the maturation of c-type cytochromes in the Euglenozoa; it also hints at a distinctive redox environment in the mitochondrial intermembrane space of trypanosomes. Surprisingly, Saccharomyces cerevisiae cytochrome c heme lyase (the yeast cytochrome c biogenesis system) cannot efficiently mature Trypanosoma brucei cytochrome c or a CXXCH variant when expressed in the cytoplasm of Escherichia coli, despite their great structural similarity to yeast cytochrome c, suggesting that heme lyase requires specific recognition features in the apocytochrome.
Structure of a trypanosomatid mitochondrial cytochrome c with heme attached via only one thioether bond and implications for the substrate recognition requirements of heme lyase.,Fulop V, Sam KA, Ferguson SJ, Ginger ML, Allen JW FEBS J. 2009 May;276(10):2822-32. PMID:19459937[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fulop V, Sam KA, Ferguson SJ, Ginger ML, Allen JW. Structure of a trypanosomatid mitochondrial cytochrome c with heme attached via only one thioether bond and implications for the substrate recognition requirements of heme lyase. FEBS J. 2009 May;276(10):2822-32. PMID:19459937 doi:10.1111/j.1742-4658.2009.07005.x
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