Published January 1, 2021
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Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
Creators
- 1. Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey
- 2. Stanford Univ, Dept Earth Syst Sci, Stanford, CA 94305 USA
- 3. Nutcracker Therapeut Inc, 5858 Horton St,Suite 540, Emeryville, CA 94608 USA
- 4. Lawrence Berkeley Natl Lab, US DOE, Joint Genome Inst, Berkeley, CA 94720 USA
Description
The 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.
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