View source for 4zid


==Dimeric Hydrogenobacter thermophilus cytochrome c552 obtained from Escherichia coli==
<StructureSection load='4zid' size='340' side='right'caption='[[4zid]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus_TK-6 Hydrogenobacter thermophilus TK-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZID 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]] 1.8&#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=4zid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zid OCA], [https://pdbe.org/4zid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zid RCSB], [https://www.ebi.ac.uk/pdbsum/4zid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zid ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CY552_HYDTT CY552_HYDTT] Reacts with hydrogenase.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Knowledge on domain swapping in vitro is increasing, but domain swapping may not occur regularly in vivo, and its information in cells is limited. Herein, we show that domain-swapped oligomers of a thermostable c-type cytochrome, Hydrogenobacter thermophilus cyt c552, are formed in E. coli which expresses cyt c552. The region containing the N-terminal alpha-helix and heme was domain-swapped between protomers in the dimer formed in E. coli. The amount of cyt c552 oligomers increased in E. coli as the cyt c552 concentration was increased, whereas that of high-order oligomers decreased in the order of decrease in protein stability, indicating that domain swapping decreases in cells when the protein stability decreases. Apo cyt c552 was detected in the cyt c552 oligomer formed in E. coli, but not in that of the A5F/M11V/Y32F/Y41E/I76V mutant. The cyt c552 oligomer containing its apo protein may form at the periplasm, since the apo protein detected by mass measurements did not contain the signal peptide. These results show that domain-swapped cyt c552 oligomers were formed in E. coli, owing to the stability of the transient oligomer containing the apo protein before heme attachment. This is an indication that exceedingly stable proteins may have disadvantages forming domain-swapped oligomers in cells.

Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells.,Hayashi Y, Yamanaka M, Nagao S, Komori H, Higuchi Y, Hirota S Sci Rep. 2016 Feb 3;6:19334. doi: 10.1038/srep19334. PMID:26838805<ref>PMID:26838805</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zid" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hydrogenobacter thermophilus TK-6]]
[[Category: Large Structures]]
[[Category: Hayashi Y]]
[[Category: Higuchi Y]]
[[Category: Hirota S]]
[[Category: Komori H]]
[[Category: Nagao S]]
[[Category: Yamanaka M]]