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Abstract
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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1 Koc University, Department of Molecular Biology and Genetics, Istanbul, Turkey (GRID:grid.15876.3d) (ISNI:0000000106887552)
2 Stanford University, Department of Earth System Science, Stanford, USA (GRID:grid.168010.e) (ISNI:0000000419368956)
3 Nutcracker Therapeutics, Emeryville, USA (GRID:grid.15876.3d)
4 Lawrence Berkeley National Laboratory, The US Department of Energy, Joint Genome Institute, Berkeley, USA (GRID:grid.184769.5) (ISNI:0000 0001 2231 4551)
5 Stanford University, Department of Structural Biology, Palo Alto, USA (GRID:grid.168010.e) (ISNI:0000000419368956); SLAC National Laboratory, Biosciences Division, Menlo Park, USA (GRID:grid.445003.6) (ISNI:0000 0001 0725 7771)
6 Koc University, Department of Molecular Biology and Genetics, Istanbul, Turkey (GRID:grid.15876.3d) (ISNI:0000000106887552); SLAC National Laboratory, Stanford PULSE Institute, Menlo Park, USA (GRID:grid.445003.6) (ISNI:0000 0001 0725 7771)