6wnd | pdb_00006wnd

Structure of the Rieske non-heme iron oxygenase GxtA with dideoxysaxitoxin bound

spinqualitylabelsall models 6wnd, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wnd is a 3 chain structure with sequence from Microseira wollei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.18Å Ligands: CL, FE, FES, GOL, U5A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C3RVP5_9CYAN Publication Abstract from PubMed Biocatalysts that perform C-H hydroxylation exhibit exceptional substrate specificity and site-selectivity, often through the use of high valent oxidants to activate these inert bonds. Rieske oxygenases are examples of enzymes with the ability to perform precise mono- or dioxygenation reactions on a variety of substrates. Understanding the structural features of Rieske oxygenases responsible for control over selectivity is essential to enable the development of this class of enzymes for biocatalytic applications. Decades of research has illuminated the critical features common to Rieske oxygenases, however, structural information for enzymes that functionalize diverse scaffolds is limited. Here, we report the structures of two Rieske monooxygenases involved in the biosynthesis of paralytic shellfish toxins (PSTs), SxtT and GxtA, adding to the short list of structurally characterized Rieske oxygenases. Based on these structures, substrate-bound structures, and mutagenesis experiments, we implicate specific residues in substrate positioning and the divergent reaction selectivity observed in these two enzymes. Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.,Lukowski AL, Liu J, Bridwell-Rabb J, Narayan ARH Nat Commun. 2020 Jun 12;11(1):2991. doi: 10.1038/s41467-020-16729-0. PMID:32532989 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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