5zbm | pdb_00005zbm

Structure of glycolate oxidase containing FMN from Nicotiana benthamiana

spinqualitylabelsall models 5zbm, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zbm is a 2 chain structure with sequence from Nicotiana benthamiana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E1AXT8_NICBE Publication Abstract from PubMed Glycolate oxidase (GOX), a flavin mononucleotide (FMN)-dependent enzyme, modulates reactive oxygen species-mediated signal transduction in green plants. It has been a target protein for crop improvement because of performing a key step in photorespiration that causes the energy losses. In human, GOX is involved in the production of oxalate, which is a key metabolite in the formation of kidney stone. Here, we report the first apo-GOX structure and its complex structure with cofactor FMN from Nicotiana benthamiana by X-ray crystallography. The binding of FMN induces a pronounced conformational change of GOX tetramer. Interestingly, a conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity. Combined with enzymatic experiments and biophysical analyses, we provide new insights in the molecular mechanism of regulating GOX biological activity reversibly and new methods of agricultural production and clinical application. Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN.,Liu Y, Wu W, Chen Z Biochem Biophys Res Commun. 2018 Sep 18;503(4):3050-3056. doi:, 10.1016/j.bbrc.2018.08.092. Epub 2018 Aug 22. PMID:30143257 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycolate oxidase 3D structures

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