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7plm
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7plm is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM reconstruction of pyruvate ferredoxin oxidoreductase (PFOR) in anaerobic conditions== | |
| + | <StructureSection load='7plm' size='340' side='right'caption='[[7plm]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == 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> | ||
| + | </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='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='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> | ||
| + | </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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7plm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyruvate synthase]] | ||
| + | [[Category: Arragain, B]] | ||
| + | [[Category: Camps, J C.Fontecilla]] | ||
| + | [[Category: Cherrier, M V]] | ||
| + | [[Category: Fenel, D]] | ||
| + | [[Category: Martin, L]] | ||
| + | [[Category: Neumann, E]] | ||
| + | [[Category: Nicolet, Y]] | ||
| + | [[Category: Schoehn, G]] | ||
| + | [[Category: Vernede, X]] | ||
| + | [[Category: 4fe-4]] | ||
| + | [[Category: Anaerobic]] | ||
| + | [[Category: Electron transport]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Pyruvate catabolism]] | ||
Current revision
CryoEM reconstruction of pyruvate ferredoxin oxidoreductase (PFOR) in anaerobic conditions
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