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| | <StructureSection load='6o0b' size='340' side='right'caption='[[6o0b]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6o0b' size='340' side='right'caption='[[6o0b]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o0b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azovd Azovd]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O0B FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nifH, Avin_01380 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322710 AZOVD])</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='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'>[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> |
| - | <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=6o0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o0b OCA], [http://pdbe.org/6o0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o0b RCSB], [http://www.ebi.ac.uk/pdbsum/6o0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o0b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Azovd]] | + | [[Category: Azotobacter vinelandii DJ]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitrogenase]]
| + | [[Category: Hu Y]] |
| - | [[Category: Hu, Y]] | + | [[Category: Kang W]] |
| - | [[Category: Kang, W]] | + | [[Category: Lee CC]] |
| - | [[Category: Lee, C C]] | + | [[Category: Rettberg LA]] |
| - | [[Category: Rettberg, L A]] | + | [[Category: Ribbe MW]] |
| - | [[Category: Ribbe, M W]] | + | [[Category: Stiebritz MT]] |
| - | [[Category: Stiebritz, M T]] | + | |
| - | [[Category: Iron protein]]
| + | |
| - | [[Category: Iron-sulfur cluster]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rettberg LA, Stiebritz MT, Kang W, Lee CC, Ribbe MW, Hu Y. Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein. Chemistry. 2019 Oct 11;25(57):13078-13082. doi: 10.1002/chem.201903387. Epub 2019, Sep 4. PMID:31402524 doi:http://dx.doi.org/10.1002/chem.201903387
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