5wid

Structure of a flavodoxin from the domain Archaea

spinqualitylabelsall models 5wid, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wid is a 3 chain structure with sequence from Methanosarcina acetivorans C2A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.681Å Ligands: ACT, FMN, MRD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8TPV5_METAC Publication Abstract from PubMed Flavodoxins, electron transfer proteins essential for diverse metabolisms in microbes from the domain Bacteria, are extensively characterized. Remarkably, although genomic annotations of flavodoxins are widespread in microbes from the domain Archaea, none have been isolated and characterized. Herein is described the structural, biochemical, and physiological characterization of an unusual flavodoxin (FldA) from Methanosarcina acetivorans, an acetate-utilizing methane-producing microbe of the domain Archaea In contrast to all flavodoxins, FldA is homodimeric, markedly less acidic, and stabilizes an anionic semiquinone. The crystal structure reveals an flavin mononucleotide (FMN) binding site unique from all other flavodoxins that provides a rationale for stabilization of the anionic semiquinone and a remarkably low reduction potentials for both the oxidized/semiquinone (-301 mV) and semiquinone/hydroquinone couples (-464 mV). FldA is up-regulated in acetate-grown versus methanol-grown cells and shown here to substitute for ferredoxin in mediating the transfer of low potential electrons from the carbonyl of acetate to the membrane-bound electron transport chain that generates ion gradients driving ATP synthesis. FldA offers potential advantages over ferredoxin by (i) sparing iron for abundant iron-sulfur proteins essential for acetotrophic growth and (ii) resilience to oxidative damage. Structure and function of an unusual flavodoxin from the domain Archaea.,Prakash D, Iyer PR, Suharti S, Walters KA, Santiago-Martinez MG, Golbeck JH, Murakami KS, Ferry JG Proc Natl Acad Sci U S A. 2019 Dec 17;116(51):25917-25922. doi:, 10.1073/pnas.1908578116. Epub 2019 Dec 4. PMID:31801875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flavodoxin 3D structures

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