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7ZC6

Na+ - translocating ferredoxin: NAD+ reductase (Rnf) of C. tetanomorphum

Summary for 7ZC6
Entry DOI10.2210/pdb7zc6/pdb
EMDB information14622
DescriptorRnfA, RIBOFLAVIN, RnfB, ... (10 entities in total)
Functional Keywordsrnf, flavin, iron-sulfur cluster, sodium ion translocation, anaerobic energy metabolism, oxidoreductase, electron transport, redox-coupled sodium pump, flavoprotein
Biological sourceClostridium tetanomorphum
More
Total number of polymer chains6
Total formula weight173737.84
Authors
Ermler, U.,Vitt, S.,Buckel, W. (deposition date: 2022-03-25, release date: 2022-09-28, Last modification date: 2024-10-23)
Primary citationVitt, S.,Prinz, S.,Eisinger, M.,Ermler, U.,Buckel, W.
Purification and structural characterization of the Na + -translocating ferredoxin: NAD + reductase (Rnf) complex of Clostridium tetanomorphum.
Nat Commun, 13:6315-6315, 2022
Cited by
PubMed Abstract: Various microbial metabolisms use H/Na-translocating ferredoxin:NAD reductase (Rnf) either to exergonically oxidize reduced ferredoxin by NAD for generating a transmembrane electrochemical potential or reversely to exploit the latter for producing reduced ferredoxin. For cryo-EM structural analysis, we elaborated a quick four-step purification protocol for the Rnf complex from Clostridium tetanomorphum and integrated the homogeneous and active enzyme into a nanodisc. The obtained 4.27 Å density map largely allows chain tracing and redox cofactor identification complemented by biochemical data from entire Rnf and single subunits RnfB, RnfC and RnfG. On this basis, we postulated an electron transfer route between ferredoxin and NAD via eight [4Fe-4S] clusters, one Fe ion and four flavins crossing the cell membrane twice related to the pathway of NADH:ubiquinone reductase. Redox-coupled Na translocation is provided by orchestrating Na uptake/release, electrostatic effects of the assumed membrane-integrated FMN semiquinone anion and accompanied polypeptide rearrangements mediated by different redox steps.
PubMed: 36274063
DOI: 10.1038/s41467-022-34007-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.27 Å)
Structure validation

237735

數據於2025-06-18公開中

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