View source for 7adr


==CO bound as bridging ligand at the active site of vanadium nitrogenase VFe protein==
<StructureSection load='7adr' size='340' side='right'caption='[[7adr]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7adr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ADR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ADR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=7adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7adr OCA], [https://pdbe.org/7adr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7adr RCSB], [https://www.ebi.ac.uk/pdbsum/7adr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7adr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VNFD_AZOVI VNFD_AZOVI] This vanadium-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 ==
Nitrogenases reduce N 2 , the most abundant element in Earth's atmosphere that is otherwise resistant to chemical conversions due to its stable triple bond. Vanadium nitrogenase stands out in that it additionally processes carbon monoxide, a known inhibitor of the more prominent molybdenum nitrogenase. The reduction of CO leads to the formation of hydrocarbon products, holding the potential for biotechnological applications in analogy to the industrial Fischer-Tropsch process. Here we report the most highly resolved structure of vanadium nitrogenase to date at 1.0 A resolution, with CO bound to the active site cofactor after catalytic turnover. CO bridges iron ions Fe2 and Fe6, replacing sulfide S2B, in a binding mode that is in line with previous reports on the CO complex of molybdenum nitrogenase. We discuss the structural consequences of continued turnover when CO is removed, which involve the replacement of CO possibly by OH - , the movement of Q176 D and K391 D , the return of sulfide and the emergence of two additional water molecules that are absent in the CO-bound state.

CO binding to the FeV Cofactor of CO-reducing Vanadium Nitrogenase at Atomic Resolution.,Rohde M, Grunau K, Einsle O Angew Chem Int Ed Engl. 2020 Sep 11. doi: 10.1002/anie.202010790. PMID:32915491<ref>PMID:32915491</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7adr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Large Structures]]
[[Category: Einsle O]]
[[Category: Grunau K]]
[[Category: Rohde M]]