5gyr: Difference between revisions
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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 [http://en.wikipedia.org/wiki/Allvd Allvd]. 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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bbh|1bbh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bbh|1bbh]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cycA, Alvin_2765 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</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'>[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> | ||
</table> | </table> | ||
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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: Allvd]] | |||
[[Category: Large Structures]] | |||
[[Category: Higuchi, Y]] | [[Category: Higuchi, Y]] | ||
[[Category: Hirota, S]] | [[Category: Hirota, S]] | ||
Revision as of 13:49, 2 October 2019
Tetrameric Allochromatium vinosum cytochrome c'Tetrameric Allochromatium vinosum cytochrome c'
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 PubMedThe 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 AlsoReferences
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