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| | ==Tetrameric Allochromatium vinosum cytochrome c'== | | ==Tetrameric Allochromatium vinosum cytochrome c'== |
| - | <StructureSection load='5gyr' size='340' side='right' caption='[[5gyr]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='5gyr' size='340' side='right'caption='[[5gyr]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gyr]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GYR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gyr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum_DSM_180 Allochromatium vinosum DSM 180]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GYR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bbh|1bbh]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gyr OCA], [http://pdbe.org/5gyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gyr RCSB], [http://www.ebi.ac.uk/pdbsum/5gyr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gyr 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=5gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gyr OCA], [https://pdbe.org/5gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gyr RCSB], [https://www.ebi.ac.uk/pdbsum/5gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gyr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYCP_ALLVD CYCP_ALLVD]] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. | + | [https://www.uniprot.org/uniprot/CYCP_ALLVD CYCP_ALLVD] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5gyr" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5gyr" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Higuchi, Y]] | + | [[Category: Allochromatium vinosum DSM 180]] |
| - | [[Category: Hirota, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Hoshizumi, M]] | + | [[Category: Higuchi Y]] |
| - | [[Category: Nagao, S]] | + | [[Category: Hirota S]] |
| - | [[Category: Nakayama, R]] | + | [[Category: Hoshizumi M]] |
| - | [[Category: Shibata, N]] | + | [[Category: Nagao S]] |
| - | [[Category: Yamanaka, M]] | + | [[Category: Nakayama R]] |
| - | [[Category: Electron transport]]
| + | [[Category: Shibata N]] |
| | + | [[Category: Yamanaka M]] |
| Structural highlights
Function
CYCP_ALLVD Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Publication Abstract from PubMed
The number of artificial protein supramolecules has been increasing; however, control of protein oligomer formation remains challenging. Cytochrome c' from Allochromatium vinosum (AVCP) is a homodimeric protein in its native form, where its protomer exhibits a four-helix bundle structure containing a covalently bound five-coordinate heme as a gas binding site. AVCP exhibits a unique reversible dimer-monomer transition according to the absence and presence of CO. Herein, domain-swapped dimeric AVCP was constructed and utilized to form a tetramer and high-order oligomers. The X-ray crystal structure of oxidized tetrameric AVCP consisted of two monomer subunits and one domain-swapped dimer subunit, which exchanged the region containing helices alphaA and alphaB between protomers. The active site structures of the domain-swapped dimer subunit and monomer subunits in the tetramer were similar to those of the monomer subunits in the native dimer. The subunit-subunit interactions at the interfaces of the domain-swapped dimer and monomer subunits in the tetramer were also similar to the subunit-subunit interaction in the native dimer. Reduced tetrameric AVCP dissociated to a domain-swapped dimer and two monomers upon CO binding. Without monomers, the domain-swapped dimers formed tetramers, hexamers, and higher-order oligomers in the absence of CO, whereas the oligomers dissociated to domain-swapped dimers in the presence of CO, demonstrating that the domain-swapped dimer maintains the CO-induced subunit dissociation behavior of native ACVP. These results suggest that protein oligomer formation may be controlled by utilizing domain swapping for a dimer-monomer transition protein.
Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.,Yamanaka M, Hoshizumi M, Nagao S, Nakayama R, Shibata N, Higuchi Y, Hirota S Protein Sci. 2017 Mar;26(3):464-474. doi: 10.1002/pro.3090. Epub 2017 Feb 14. PMID:27883268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamanaka M, Hoshizumi M, Nagao S, Nakayama R, Shibata N, Higuchi Y, Hirota S. Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers. Protein Sci. 2017 Mar;26(3):464-474. doi: 10.1002/pro.3090. Epub 2017 Feb 14. PMID:27883268 doi:http://dx.doi.org/10.1002/pro.3090
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