6WND

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

Summary for 6WND

• Entry DOI: 10.2210/pdb6wnd/pdb
• Related: 6WN3
• Descriptor: SxtDIOX, FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (7 entities in total)
• Functional Keywords: saxitoxin, rieske oxygenase, metalloprotein, natural products, biosynthetic protein
• Biological source: Microseira wollei
• Total number of polymer chains: 3
• Total formula weight: 117658.15

Authors

Bridwell-Rabb, J.,Liu, J. (deposition date: 2020-04-22, release date: 2020-06-17, Last modification date: 2023-10-18)

Primary citation

Lukowski, A.L.,Liu, J.,Bridwell-Rabb, J.,Narayan, A.R.H.
Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.
Nat Commun, 11:2991-2991, 2020

PubMed Abstract: 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.

PubMed: 32532989
DOI: 10.1038/s41467-020-16729-0

Experimental method

X-RAY DIFFRACTION (2.18 Å)