8ahx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the nitrogen-fixation associated NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii== | |
| + | <StructureSection load='8ahx' size='340' side='right'caption='[[8ahx]], [[Resolution|resolution]] 3.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ahx]] is a 7 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=8AHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AHX FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.11Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</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=8ahx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ahx OCA], [https://pdbe.org/8ahx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ahx RCSB], [https://www.ebi.ac.uk/pdbsum/8ahx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ahx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C1DMA8_AZOVD C1DMA8_AZOVD] Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.[HAMAP-Rule:MF_00459] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biological nitrogen fixation requires substantial metabolic energy in form of ATP as well as low-potential electrons that must derive from central metabolism. During aerobic growth, the free-living soil diazotroph Azotobacter vinelandii transfers electrons from the key metabolite NADH to the low-potential ferredoxin FdxA that serves as a direct electron donor to the dinitrogenase reductases. This process is mediated by the RNF complex that exploits the proton motive force over the cytoplasmic membrane to lower the midpoint potential of the transferred electron. Here we report the cryogenic electron microscopy structure of the nitrogenase-associated RNF complex of A. vinelandii, a seven-subunit membrane protein assembly that contains four flavin cofactors and six iron-sulfur centers. Its function requires the strict coupling of electron and proton transfer but also involves major conformational changes within the assembly that can be traced with a combination of electron microscopy and modeling. | ||
| - | + | Architecture of the RNF1 complex that drives biological nitrogen fixation.,Zhang L, Einsle O Nat Chem Biol. 2024 Aug;20(8):1078-1085. doi: 10.1038/s41589-024-01641-1. Epub , 2024 Jun 18. PMID:38890433<ref>PMID:38890433</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8ahx" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii DJ]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Einsle O]] | ||
| + | [[Category: Zhang L]] | ||
Current revision
Cryo-EM structure of the nitrogen-fixation associated NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii
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