View source for 6aiq


==High resolution structure of recombinant high-potential iron-sulfur protein==
<StructureSection load='6aiq' size='340' side='right'caption='[[6aiq]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6aiq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AIQ 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]] 0.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6aiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aiq OCA], [https://pdbe.org/6aiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aiq RCSB], [https://www.ebi.ac.uk/pdbsum/6aiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aiq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HIP_THETI HIP_THETI] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high-resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X-ray structure of perdeuterated high-potential iron-sulfur protein (HiPIP) at a high resolution of 0.85 a resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high-resolution neutron crystallography.

Characterization of perdeuterated high-potential iron-sulfur protein with high-resolution X-ray crystallography.,Hanazono Y, Takeda K, Miki K Proteins. 2019 Jul 31. doi: 10.1002/prot.25793. PMID:31365157<ref>PMID:31365157</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aiq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermochromatium tepidum]]
[[Category: Hanazono Y]]
[[Category: Miki K]]
[[Category: Takeda K]]