6o0b
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein== | |
| + | <StructureSection load='6o0b' size='340' side='right'caption='[[6o0b]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6o0b]] is a 2 chain structure with sequence from [https://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=6O0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O0B 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6o0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0b OCA], [https://pdbe.org/6o0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o0b RCSB], [https://www.ebi.ac.uk/pdbsum/6o0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C1DGZ6_AZOVD C1DGZ6_AZOVD] The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Fe protein of nitrogenase catalyzes the ambient reduction of CO2 when its cluster is present in the all-ferrous, [Fe4 S4 ](0) oxidation state. Here, we report a combined structural and theoretical study that probes the unique reactivity of the all-ferrous Fe protein toward CO2 . Structural comparisons of the Azotobacter vinelandii Fe protein in the [Fe4 S4 ](0) and [Fe4 S4 ](+) states point to a possible asymmetric functionality of a highly conserved Arg pair in CO2 binding and reduction. Density functional theory (DFT) calculations provide further support for the asymmetric coordination of O by the "proximal" Arg and binding of C to a unique Fe atom of the all-ferrous cluster, followed by donation of protons by the proximate guanidinium group of Arg that eventually results in the scission of a C-O bond. These results provide important mechanistic and structural insights into CO2 activation by a surface-exposed, scaffold-held [Fe4 S4 ] cluster. | ||
| - | + | Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein.,Rettberg LA, Stiebritz MT, Kang W, Lee CC, Ribbe MW, Hu Y Chemistry. 2019 Oct 11;25(57):13078-13082. doi: 10.1002/chem.201903387. Epub 2019, Sep 4. PMID:31402524<ref>PMID:31402524</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6o0b" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Nitrogenase 3D structures|Nitrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii DJ]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hu Y]] | ||
| + | [[Category: Kang W]] | ||
| + | [[Category: Lee CC]] | ||
| + | [[Category: Rettberg LA]] | ||
| + | [[Category: Ribbe MW]] | ||
| + | [[Category: Stiebritz MT]] | ||
Current revision
Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein
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