3wsi: Difference between revisions
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New page: '''Unreleased structure''' The entry 3wsi is ON HOLD Authors: Fujishiro, T., Ermler, U., Shima, S. Description: EDTA-treated, reduced HcgD from Methanocaldococcus jannaschii |
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==EDTA-treated, reduced HcgD from Methanocaldococcus jannaschii== | |||
<StructureSection load='3wsi' size='340' side='right'caption='[[3wsi]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wsi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSI 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3wsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsi OCA], [https://pdbe.org/3wsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsi RCSB], [https://www.ebi.ac.uk/pdbsum/3wsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsi ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HcgD, a homolog of the ubiquitous Nif3-like protein family, is found in a gene cluster involved in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase. The presented crystal structure and biochemical analyses indicated that HcgD has a dinuclear iron-center, which provides a pronounced binding site for anionic ligands. HcgD contains a stronger and a weaker bound iron; the latter being removable by chelating reagents preferentially in the oxidized state. Therefore, we propose HcgD as an iron chaperone in FeGP cofactor biosynthesis, which might also stimulate investigations on the functionally unknown but physiologically important eukaryotic Nif3-like protein family members. | |||
A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis.,Fujishiro T, Ermler U, Shima S FEBS Lett. 2014 Aug 25;588(17):2789-93. doi: 10.1016/j.febslet.2014.05.059. Epub , 2014 Jun 12. PMID:24931373<ref>PMID:24931373</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wsi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanocaldococcus jannaschii DSM 2661]] | |||
[[Category: Ermler U]] | |||
[[Category: Fujishiro T]] | |||
[[Category: Shima S]] | |||
Latest revision as of 13:25, 8 November 2023
EDTA-treated, reduced HcgD from Methanocaldococcus jannaschii
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