7aiz: Difference between revisions

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<table><tr><td colspan='2'>[[7aiz]] 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=7AIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AIZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[7aiz]] 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=7AIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AIZ 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]] 1.05&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05&#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=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=D6N:FeV'>D6N</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='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=7aiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aiz OCA], [https://pdbe.org/7aiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aiz RCSB], [https://www.ebi.ac.uk/pdbsum/7aiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aiz 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=7aiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aiz OCA], [https://pdbe.org/7aiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aiz RCSB], [https://www.ebi.ac.uk/pdbsum/7aiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aiz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.
[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 ==
Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C(2)H(4)), implying a C-C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 A resolution, with one mu-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion.
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle.,Rohde M, Laun K, Zebger I, Stripp ST, Einsle O Sci Adv. 2021 May 28;7(22):eabg4474. doi: 10.1126/sciadv.abg4474. Print 2021 May. PMID:34049880<ref>PMID:34049880</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7aiz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 09:37, 16 September 2026

Vanadium nitrogenase VFe protein, high CO state

7aiz, resolution 1.05Å

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