6WNC

Structure of the Rieske non-heme iron oxygenase GxtA

6WNC の概要

• エントリーDOI: 10.2210/pdb6wnc/pdb
• 関連するPDBエントリー: 6WN3
• 分子名称: SxtDIOX, FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: saxitoxin, rieske oxygenase, metalloprotein, natural products, biosynthetic protein
• 由来する生物種: Microseira wollei
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 115609.34

構造登録者

Bridwell-Rabb, J.,Liu, J. (登録日: 2020-04-22, 公開日: 2020-06-17, 最終更新日: 2023-10-18)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)