8p8g
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Nitrogenase MoFe protein from A. vinelandii beta double mutant D353G/D357G== | |
| + | <StructureSection load='8p8g' size='340' side='right'caption='[[8p8g]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8p8g]] is a 4 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=8P8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P8G 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]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1CL:FE(8)-S(7)+CLUSTER,+OXIDIZED'>1CL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=8p8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p8g OCA], [https://pdbe.org/8p8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p8g RCSB], [https://www.ebi.ac.uk/pdbsum/8p8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p8g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C1DGZ7_AZOVD C1DGZ7_AZOVD] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.[ARBA:ARBA00002621] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The biological N(2)-fixation process is catalyzed exclusively by metallocofactor-containing nitrogenases. Structural and spectroscopic studies highlighted the presence of an additional mononuclear metal-binding (MMB) site, which can coordinate Fe in addition to the two metallocofactors required for the reaction. This MMB site is located 15-A from the active site, at the interface of two NifK subunits. The enigmatic function of the MMB site and its implications for metallocofactor installation, catalysis, electron transfer, or structural stability are investigated in this work. The axial ligands coordinating the additional Fe are almost universally conserved in Mo-nitrogenases, but a detailed observation of the available structures indicates a variation in occupancy or a metal substitution. A nitrogenase variant in which the MMB is disrupted was generated and characterized by X-ray crystallography, biochemistry, and enzymology. The crystal structure refined to 1.55-A revealed an unambiguous loss of the metal site, also confirmed by an absence of anomalous signal for Fe. The position of the surrounding side chains and the overall architecture are superposable with the wild-type structure. Accordingly, the biochemical and enzymatic properties of the variant are similar to those of the wild-type nitrogenase, indicating that the MMB does not impact nitrogenase's activity and stability in vitro. | ||
| - | + | The Mononuclear Metal-Binding Site of Mo-Nitrogenase Is Not Required for Activity.,Cadoux C, Maslac N, Di Luzio L, Ratcliff D, Gu W, Wagner T, Milton RD JACS Au. 2023 Nov 6;3(11):2993-2999. doi: 10.1021/jacsau.3c00567. eCollection , 2023 Nov 27. PMID:38034976<ref>PMID:38034976</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8p8g" style="background-color:#fffaf0;"></div> |
| - | [[Category: Maslac | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii DJ]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Maslac N]] | ||
| + | [[Category: Wagner T]] | ||
Current revision
Nitrogenase MoFe protein from A. vinelandii beta double mutant D353G/D357G
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