7plm: Difference between revisions

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<StructureSection load='7plm' size='340' side='right'caption='[[7plm]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='7plm' size='340' side='right'caption='[[7plm]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7plm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PLM FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PLM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b0p|1b0p]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_synthase Pyruvate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] </span></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=7plm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7plm OCA], [https://pdbe.org/7plm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7plm RCSB], [https://www.ebi.ac.uk/pdbsum/7plm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7plm ProSAT]</span></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=7plm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7plm OCA], [https://pdbe.org/7plm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7plm RCSB], [https://www.ebi.ac.uk/pdbsum/7plm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7plm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/PFOR_DESAF PFOR_DESAF]] Catalyzes the ferredoxin-dependent oxidative decarboxylation of pyruvate. Required for the transfer of electrons from pyruvate to ferredoxin (PubMed:9294422, PubMed:7612653). Ferredoxin I and ferredoxin II, which are single 4Fe-4S cluster ferredoxins are the most effective electron carriers of POR (PubMed:7612653).<ref>PMID:7612653</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive to oxygen-induced degradation. Consequently, their study usually requires strict anaerobic conditions. Although X-ray crystallography has been the method of choice for solving macromolecular structures for many years, recently electron microscopy has also become an increasingly powerful structure-solving technique. We have used our previous experience with cryo-crystallography to develop a method to prepare cryo-EM grids in an anaerobic chamber and have applied it to solve the structures of apoferritin and the 3 [Fe4S4]-containing pyruvate ferredoxin oxidoreductase (PFOR) at 2.40 A and 2.90 A resolution, respectively. The maps are of similar quality to the ones obtained under air, thereby validating our method as an improvement in the structural investigation of oxygen-sensitive metalloproteins by cryo-EM.


Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy.,Cherrier MV, Vernede X, Fenel D, Martin L, Arragain B, Neumann E, Fontecilla-Camps JC, Schoehn G, Nicolet Y Biomolecules. 2022 Mar 12;12(3). pii: biom12030441. doi: 10.3390/biom12030441. PMID:35327633<ref>PMID:35327633</ref>
==See Also==
 
*[[Pyruvate-ferredoxin oxidoreductase|Pyruvate-ferredoxin oxidoreductase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7plm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyruvate synthase]]
[[Category: Arragain B]]
[[Category: Arragain, B]]
[[Category: Cherrier MV]]
[[Category: Camps, J C.Fontecilla]]
[[Category: Fenel D]]
[[Category: Cherrier, M V]]
[[Category: Fontecilla Camps JC]]
[[Category: Fenel, D]]
[[Category: Martin L]]
[[Category: Martin, L]]
[[Category: Neumann E]]
[[Category: Neumann, E]]
[[Category: Nicolet Y]]
[[Category: Nicolet, Y]]
[[Category: Schoehn G]]
[[Category: Schoehn, G]]
[[Category: Vernede X]]
[[Category: Vernede, X]]
[[Category: 4fe-4]]
[[Category: Anaerobic]]
[[Category: Electron transport]]
[[Category: Oxidoreductase]]
[[Category: Pyruvate catabolism]]
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