Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.
Bacterial Proteins
/ chemistry
Binding Sites
/ genetics
Biocatalysis
Catalytic Domain
Cyanobacteria
/ enzymology
Genetic Variation
Hydroxylation
Iron-Sulfur Proteins
/ chemistry
Kinetics
Mixed Function Oxygenases
/ chemistry
Models, Molecular
Oxygenases
/ chemistry
Protein Conformation
Protein Multimerization
Substrate Specificity
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
12 06 2020
12 06 2020
Historique:
received:
25
02
2020
accepted:
15
05
2020
entrez:
14
6
2020
pubmed:
14
6
2020
medline:
25
8
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32532989
doi: 10.1038/s41467-020-16729-0
pii: 10.1038/s41467-020-16729-0
pmc: PMC7293229
doi:
Substances chimiques
Bacterial Proteins
0
Iron-Sulfur Proteins
0
Mixed Function Oxygenases
EC 1.-
Oxygenases
EC 1.13.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2991Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM124880
Pays : United States
Organisme : NINDS NIH HHS
ID : F31 NS111906
Pays : United States
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