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| | ==Reduced HcgD from Methanocaldococcus jannaschii== | | ==Reduced HcgD from Methanocaldococcus jannaschii== |
| - | <StructureSection load='3wse' size='340' side='right' caption='[[3wse]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3wse' size='340' side='right'caption='[[3wse]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wse]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WSE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wse]] 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=3WSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wsd|3wsd]], [[3wsf|3wsf]], [[3wsg|3wsg]], [[3wsh|3wsh]], [[3wsi|3wsi]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0927 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</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=3wse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wse OCA], [https://pdbe.org/3wse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wse RCSB], [https://www.ebi.ac.uk/pdbsum/3wse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wse ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wse OCA], [http://pdbe.org/3wse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wse RCSB], [http://www.ebi.ac.uk/pdbsum/3wse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wse ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Metja]] | + | [[Category: Large Structures]] |
| - | [[Category: Ermler, U]] | + | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| - | [[Category: Fujishiro, T]] | + | [[Category: Ermler U]] |
| - | [[Category: Shima, S]] | + | [[Category: Fujishiro T]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Shima S]] |
| - | [[Category: Nif3-related protein]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujishiro T, Ermler U, Shima S. A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis. FEBS Lett. 2014 Aug 25;588(17):2789-93. doi: 10.1016/j.febslet.2014.05.059. Epub , 2014 Jun 12. PMID:24931373 doi:http://dx.doi.org/10.1016/j.febslet.2014.05.059
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