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.

Details

Title
Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
Author
Destan Ebru 1 ; Yuksel Busra 1 ; Tolar, Bradley B 2 ; Ayan Esra 1 ; Deutsch, Sam 3 ; Yoshikuni Yasuo 4 ; Wakatsuki Soichi 5 ; Francis, Christopher A 2 ; DeMirci Hasan 6 

 Koc University, Department of Molecular Biology and Genetics, Istanbul, Turkey (GRID:grid.15876.3d) (ISNI:0000000106887552) 
 Stanford University, Department of Earth System Science, Stanford, USA (GRID:grid.168010.e) (ISNI:0000000419368956) 
 Nutcracker Therapeutics, Emeryville, USA (GRID:grid.15876.3d) 
 Lawrence Berkeley National Laboratory, The US Department of Energy, Joint Genome Institute, Berkeley, USA (GRID:grid.184769.5) (ISNI:0000 0001 2231 4551) 
 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) 
 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) 
Publication year
2021
Publication date
2021
Publisher
Nature Publishing Group
e-ISSN
20452322
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2601729920
Copyright
© The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.