9fl2 | pdb_00009fl2

Crystal structure of Oscillatoria princeps pyranose oxidase

spinqualitylabelsall models 9fl2, resolution 2.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fl2 is a 4 chain structure with sequence from Oscillatoria princeps RMCB-10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.64Å Ligands: CL, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Pyranose oxidases are valuable biocatalysts, yet only a handful of bacterial pyranose oxidases are known. These bacterial enzymes exhibit noteworthy distinctions from their extensively characterized fungal counterparts, encompassing variations in substrate specificity and structural attributes. Herein a bacterial pyranose oxidase from Oscillatoria princeps (OPOx) was biochemically characterized in detail. In contrast to the fungal pyranose oxidases, OPOx could be well expressed in Escherichia coli as soluble, fully flavinylated and active oxidase. It was found to be highly thermostable (melting temperature >90 (0)C) and showed activity on glucose, exhibiting an exceptionally low K(M) value (48 muM). Elucidation of its crystal structure revealed similarities with fungal pyranose oxidases, such as being a tetramer with a large central void leading to a narrow substrate access tunnel. In the active site, the FAD cofactor is covalently bound to a histidine. OPOx displays a relatively narrow pH optimum for activity with a sharp decline at relatively basic pH values which is accompanied with a drastic change in its flavin absorbance spectrum. The pH-dependent switch in flavin absorbance features and oxidase activity was shown to be fully reversible. It is hypothesized that a glutamic acid helps to stabilize the protonated form of the histidine that is tethered to the FAD. OPOx presents itself as a valuable biocatalyst as it is highly robust, well-expressed in E. coli, shows low K(M) values for monosaccharides and has a peculiar pH dependent "on-off switch". Identification of a robust bacterial pyranose oxidase which displays an unusual pH dependence.,Santema LL, Rozeboom HJ, Borger VP, Kaya SG, Fraaije MW J Biol Chem. 2024 Oct 10:107885. doi: 10.1016/j.jbc.2024.107885. PMID:39395808 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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