View source for 3x15


==Dimeric Aquifex aeolicus cytochrome c555==
<StructureSection load='3x15' size='340' side='right'caption='[[3x15]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3x15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X15 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]] 1.6&#8491;</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=3x15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x15 OCA], [https://pdbe.org/3x15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x15 RCSB], [https://www.ebi.ac.uk/pdbsum/3x15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x15 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67504_AQUAE O67504_AQUAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c555 from hyperthermophilic bacteria Aquifex aeolicus (AA cyt c555 ) is a hyperstable protein belonging to the cyt c protein family, which possesses a unique long 310 -alpha-310 helix containing the heme-ligating Met61. Herein, we show that AA cyt c555 forms dimers by swapping the region containing the extra 310 -alpha-310 helix and C-terminal alpha-helix. The asymmetric unit of the crystal of dimeric AA cyt c555 contained two dimer structures, where the structure of the hinge region (Val53-Lys57) was different among all four protomers. Dimeric AA cyt c555 dissociated to monomers at 92 +/- 1 degrees C according to DSC measurements, showing that the dimer was thermostable. According to CD measurements, the secondary structures of dimeric AA cyt c555 were maintained at pH 2.2-11.0. CN- and CO bound to dimeric AA cyt c555 in the ferric and ferrous states, respectively, owing to the flexibility of the hinge region close to Met61 in the dimer, whereas these ligands did not bind to the monomer under the same conditions. In addition, CN- and CO bound to the oxidized and reduced dimer at neutral pH and a wide range of pH (pH 2.2-11.0), respectively, in a wide range of temperature (25-85 degrees C), owing to the thermostability and pH tolerance of the dimer. These results show that the ligand binding character of hyperstable AA cyt c555 changes upon dimerization by domain swapping.

Change in structure and ligand binding properties of hyperstable cytochrome c from Aquifex aeolicus by domain swapping.,Yamanaka M, Nagao S, Komori H, Higuchi Y, Hirota S Protein Sci. 2015 Jan 14. doi: 10.1002/pro.2627. PMID:25586341<ref>PMID:25586341</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3x15" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Hirota S]]
[[Category: Komori H]]
[[Category: Nagao S]]
[[Category: Yamanaka M]]