4d02

The crystallographic structure of Flavorubredoxin from Escherichia coli

spinqualitylabelsall models 4d02, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d02 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FE, FMN, GOL, O, PO4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Flavodiiron proteins (FDPs) are a family of enzymes endowed with bona fide oxygen- and/or nitric oxide-reductase activity, although their substrate specificity determinants remain elusive. After a comprehensive comparison of available three-dimensional structures, particularly of FDPs with a clear preference towards either O2 or NO, two main differences were identified near the diiron active site, which led to the construction of site-directed mutants of Y271 and K53 in the oxygen reducing Entamoeba histolytica EhFdp1. The biochemical and biophysical properties of these mutants were studied by UV-visible and electron paramagnetic resonance (EPR) spectroscopies coupled to potentiometry. Their reactivity with O2 and NO was analyzed by stopped-flow absorption spectroscopy and amperometric methods. These mutations, while keeping the overall properties of the redox cofactors, resulted in increased NO reductase activity and faster inactivation of the enzyme in the reaction with O2, pointing to a role of the mutated residues in substrate selectivity. Flavodiiron oxygen reductase from Entamoeba histolytica: Modulation of substrate preference by tyrosine 271 and lysine 53.,Goncalves VL, Vicente JB, Pinto L, Romao CV, Frazao C, Sarti P, Giuffre A, Teixeira M J Biol Chem. 2014 Aug 23. pii: jbc.M114.579086. PMID:25151360 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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