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6fea
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6fea is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==A. vinelandii vanadium nitrogenase, turnover state== | |
| + | <StructureSection load='6fea' size='340' side='right' caption='[[6fea]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6fea]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii_dj Azotobacter vinelandii dj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FEA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=D6N:FeV'>D6N</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5n6y|5n6y]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </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=6fea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fea OCA], [http://pdbe.org/6fea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fea RCSB], [http://www.ebi.ac.uk/pdbsum/6fea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fea ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Reduction of N2 by nitrogenases occurs at an organometallic iron cofactor that commonly also contains either molybdenum or vanadium. The well-characterized resting state of the cofactor does not bind substrate, so its mode of action remains enigmatic. Carbon monoxide was recently found to replace a bridging sulfide, but the mechanistic relevance was unclear. Here we report the structural analysis of vanadium nitrogenase with a bound intermediate, interpreted as a mu(2)-bridging, protonated nitrogen that implies the site and mode of substrate binding to the cofactor. Binding results in a flip of amino acid glutamine 176, which hydrogen-bonds the ligand and creates a holding position for the displaced sulfide. The intermediate likely represents state E6 or E7 of the Thorneley-Lowe model and provides clues to the remainder of the catalytic cycle. | ||
| - | + | A bound reaction intermediate sheds light on the mechanism of nitrogenase.,Sippel D, Rohde M, Netzer J, Trncik C, Gies J, Grunau K, Djurdjevic I, Decamps L, Andrade SLA, Einsle O Science. 2018 Mar 30;359(6383):1484-1489. doi: 10.1126/science.aar2765. PMID:29599235<ref>PMID:29599235</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6fea" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii dj]] | ||
| + | [[Category: Nitrogenase]] | ||
| + | [[Category: Einsle, O]] | ||
| + | [[Category: Sippel, D]] | ||
| + | [[Category: Iron-sulfur-enzyme]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Nitrogen fixation]] | ||
| + | [[Category: Vanadium]] | ||
Current revision
A. vinelandii vanadium nitrogenase, turnover state
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