Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
Category
Published on
Type
journal-article
Author
Ebru Destan and Busra Yuksel and Bradley B. Tolar and Esra Ayan and Sam Deutsch and Yasuo Yoshikuni and Soichi Wakatsuki and Christopher A. Francis and Hasan DeMirci
Citation
Destan, E., Yuksel, B., Tolar, B. B., Ayan, E., Deutsch, S., Yoshikuni, Y., Wakatsuki, S., Francis, C. A., & DeMirci, H. (2021). Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus. Scientific Reports, 11(1). https://doi.org/10.1038/s41598-021-02180-8
Abstract
AbstractThe ammonia-oxidizing thaumarchaeal 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle is one of the most energy-efficient CO2 fixation cycles discovered thus far. The protein encoded by Nmar_1308 (from Nitrosopumilus maritimus SCM1) is a promiscuous enzyme that catalyzes two essential reactions within the thaumarchaeal 3HP/4HB cycle, functioning as both a crotonyl-CoA hydratase (CCAH) and 3-hydroxypropionyl-CoA dehydratase (3HPD). In performing both hydratase and dehydratase activities, Nmar_1308 reduces the total number of enzymes necessary for CO2 fixation in Thaumarchaeota, reducing the overall cost for biosynthesis. Here, we present the first high-resolution crystal structure of this bifunctional enzyme with key catalytic residues in the thaumarchaeal 3HP/4HB pathway.
