View source for 5wqr


==High resolution structure of high-potential iron-sulfur protein in the reduced state==
<StructureSection load='5wqr' size='340' side='right'caption='[[5wqr]], [[Resolution|resolution]] 0.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wqr]] 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=5WQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQR 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]] 0.8&#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=5wqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqr OCA], [https://pdbe.org/5wqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wqr RCSB], [https://www.ebi.ac.uk/pdbsum/5wqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqr 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 ==
High-potential iron-sulfur protein (HiPIP) is a soluble electron carrier protein of photosynthetic bacteria with an Fe4S4 cluster. Although structural changes accompanying the electron transfer are important for understanding of the functional mechanism, the changes have not been clarified in sufficient detail. We previously reported the high-resolution crystal structures of HiPIP from a thermophilic purple bacterium Thermochromatium tepidum in the reduced state. In order to perform a detailed comparison between the structures in different redox states, the oxidized structure should also be revealed at high resolution. Therefore, in the present study we performed a crystallographic analysis of oxidized HiPIP and a structural comparison with the reduced form at a high resolution of 0.8 A. The comparison highlighted small but significant contraction in the iron-sulfur cluster. The changes in Fe-S bond lengths were similar to that predicted by theoretical calculation, although some discrepancies were also found. Almost distances between the sulfur atoms of the iron-sulfur cluster and the protein environment are elongated upon the oxidation. Positional changes of hydrogen atoms in the protein environment, such as on the amide-hydrogen of Cys75 in the proximity of the iron-sulfur cluster, were also observed in the accurate analyses. None of the water molecules exhibited significant changes in position or anisotropy of atomic displacement parameter between the two states, while the orientations of some water molecules were different.

Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 A resolution.,Ohno H, Takeda K, Niwa S, Tsujinaka T, Hanazono Y, Hirano Y, Miki K PLoS One. 2017 May 22;12(5):e0178183. doi: 10.1371/journal.pone.0178183., eCollection 2017. PMID:28542634<ref>PMID:28542634</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wqr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermochromatium tepidum]]
[[Category: Hanazono Y]]
[[Category: Hirano Y]]
[[Category: Miki K]]
[[Category: Niwa S]]
[[Category: Ohno H]]
[[Category: Takeda K]]
[[Category: Tsujinaka T]]