6op4: Difference between revisions

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-'''Unreleased structure'''
-The entry 6op4 is ON HOLD  until Paper Publication
+==Selenium-incorporated, carbon monoxide-inhibited, reactivated FeMo-cofactor of nitrogenase from Azotobacter vinelandii==
+<StructureSection load='6op4' size='340' side='right'caption='[[6op4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6op4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OP4 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6op4 OCA], [http://pdbe.org/6op4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6op4 RCSB], [http://www.ebi.ac.uk/pdbsum/6op4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6op4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/NIFD_AZOVI NIFD_AZOVI]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. [[http://www.uniprot.org/uniprot/NIFK_AZOVI NIFK_AZOVI]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The size and complexity of Mo-dependent nitrogenase, a multicomponent enzyme capable of reducing dinitrogen to ammonia, have made a detailed understanding of the FeMo cofactor (FeMoco) active site electronic structure an ongo-ing challenge. Selective substitution of sulfur by selenium in FeMoco affords a unique probe wherein local Fe-Se in-teractions can be directly interrogated via high-energy resolution fluorescence detected X-ray absorption spectroscop-ic (HERFD XAS) and extended X-ray absorption fine structure (EXAFS) studies. These studies reveal a significant asymmetry in the electronic distribution of the FeMoco, suggesting a more localized electronic structure picture than is typically assumed for iron-sulfur clusters. Supported by experimental small molecule model data in combination with time dependent density functional theory (TDDFT) calculations, the HERFD XAS data is consistent with an assign-ment of Fe2/Fe6 as an antiferromagnetically coupled diferric pair. HERFD XAS and EXAFS have also been applied to Se-substituted CO-inhibited MoFe protein, demonstrating the ability of these methods to reveal electronic and struc-tural changes that occur upon substrate binding. These results emphasize the utility of Se HERFD XAS and EXAFS for selectively probing the local electronic and geometric structure of FeMoco.
-Authors: Arias, R.J., Rees, D.C.
+Localized Electronic Structure of Nitrogenase FeMoco Re-vealed by Selenium K-edge High Resolution X-ray Absorption Spectroscopy.,Henthorn JT, Arias RJ, Koroidov S, Kroll T, Sokaras D, Bergmann U, Rees DC, DeBeer S J Am Chem Soc. 2019 Jul 29. doi: 10.1021/jacs.9b06988. PMID:31356071<ref>PMID:31356071</ref>
-Description: Selenium-incorporated, carbon monoxide-inhibited, reactivated FeMo-cofactor of nitrogenase from Azotobacter vinelandii
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Rees, D.C]]
+<div class="pdbe-citations 6op4" style="background-color:#fffaf0;"></div>
-[[Category: Arias, R.J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Azotobacter vinelandii]]
+[[Category: Large Structures]]
+[[Category: Nitrogenase]]
+[[Category: Arias, R J]]
+[[Category: Rees, D C]]
+[[Category: Carbon monoxide]]
+[[Category: Femo-cofactor]]
+[[Category: Oxidoreductase]]
+[[Category: Selenium]]