8c3m | pdb_00008c3m

Crystal structure of ferredoxin/flavodoxin NADP+ oxidoreductase 1 (FNR1) V329H mutant from Bacillus cereus

spinqualitylabelsall models 8c3m, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8c3m is a 2 chain structure with sequence from Bacillus cereus ATCC 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: ACT, FAD, OXM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q81IK1_BACCR Publication Abstract from PubMed Although bacterial thioredoxin reductase-like ferredoxin/flavodoxin NAD(P)(+) oxidoreductases (FNRs) are similar in terms of primary sequences and structures, they participate in diverse biological processes by catalyzing a range of different redox reactions. Many of the reactions are critical for the growth, survival of, and infection by pathogens, and insight into the structural basis for substrate preference, specificity, and reaction kinetics is crucial for the detailed understanding of these redox pathways. Bacillus cereus (Bc) encodes three FNR paralogs, two of which have assigned distinct biological functions in bacillithiol disulfide reduction and flavodoxin (Fld) reduction. Bc FNR2, the endogenous reductase of the Fld-like protein NrdI, belongs to a distinct phylogenetic cluster of homologous oxidoreductases containing a conserved His residue stacking the FAD cofactor. In this study, we have assigned a function to FNR1, in which the His residue is replaced by a conserved Val, in the reduction of the heme-degrading monooxygenase IsdG, ultimately facilitating the release of iron in an important iron acquisition pathway. The Bc IsdG structure was solved, and IsdG-FNR1 interactions were proposed through protein-protein docking. Mutational studies and bioinformatics analyses confirmed the importance of the conserved FAD-stacking residues on the respective reaction rates, proposing a division of FNRs into four functionally unique sequence similarity clusters likely related to the nature of this residue. Functional Diversity of Homologous Oxidoreductases-Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction.,Hammerstad M, Rugtveit AK, Dahlen S, Andersen HK, Hersleth HP Antioxidants (Basel). 2023 Jun 6;12(6):1224. doi: 10.3390/antiox12061224. PMID:37371954 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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