7jrf
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==CO-CO-BOUND NITROGENASE MOFE-PROTEIN FROM A. VINELANDII== |
| - | <StructureSection load='7jrf' size='340' side='right'caption='[[7jrf]]' scene=''> | + | <StructureSection load='7jrf' size='340' side='right'caption='[[7jrf]], [[Resolution|resolution]] 1.33Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7jrf]] is a 4 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=7JRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JRF FirstGlance]. <br> |
| - | </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=7jrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jrf OCA], [https://pdbe.org/7jrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jrf RCSB], [https://www.ebi.ac.uk/pdbsum/7jrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jrf ProSAT]</span></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]] 1.33Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICE:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICE</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7jrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jrf OCA], [https://pdbe.org/7jrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jrf RCSB], [https://www.ebi.ac.uk/pdbsum/7jrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jrf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As an approach towards unraveling the nitrogenase mechanism, we have studied the binding of CO to the active-site FeMo-cofactor. CO is not only an inhibitor of nitrogenase, but it is also a substrate, undergoing reduction to hydrocarbons (Fischer-Tropsch-type chemistry). The C-C bond forming capabilities of nitrogenase suggest that multiple CO or CO-derived ligands bind to the active site. Herein, we report a crystal structure with two CO ligands coordinated to the FeMo-cofactor of the molybdenum nitrogenase at 1.33 A resolution. In addition to the previously observed bridging CO ligand between Fe2 and Fe6 of the FeMo-cofactor, a new ligand binding mode is revealed through a second CO ligand coordinated terminally to Fe6. While the relevance of this state to nitrogenase-catalyzed reactions remains to be established, it highlights the privileged roles for Fe2 and Fe6 in ligand binding, with multiple coordination modes available depending on the ligand and reaction conditions. | ||
| + | |||
| + | Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site.,Buscagan TM, Perez KA, Maggiolo AO, Rees DC, Spatzal T Angew Chem Int Ed Engl. 2021 Mar 8;60(11):5704-5707. doi: 10.1002/anie.202015751. , Epub 2021 Jan 27. PMID:33320413<ref>PMID:33320413</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7jrf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Nitrogenase 3D structures|Nitrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Buscagan TM]] |
| + | [[Category: Maggiolo AO]] | ||
| + | [[Category: Perez KA]] | ||
| + | [[Category: Rees DC]] | ||
| + | [[Category: Spatzal T]] | ||
Current revision
CO-CO-BOUND NITROGENASE MOFE-PROTEIN FROM A. VINELANDII
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