Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 730, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2022.109391
Keywords
8-oxidation; Enoyl-CoA hydratase; 3-Hydroxyacyl-CoA dehydrogenase; Cupriavidus necator H16; Non-forming FadAB complex
Categories
Funding
- Cooperative Research Program for Agricultural Science AMP
- Technology Development, Rural Development Administration, Republic of Korea [PJ01492602]
- National Research Foundation of Korea (NRF) - Korean government [2021R1C1C2004411, 2020M3H1A1075314, 2020R1I1A1A01057880]
- National Research Foundation of Korea [2020R1I1A1A01057880, 2020M3H1A1075314, 2021R1C1C2004411] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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By determining the crystal structure of multi-functional enoyl-CoA hydratase from Cupriavidus necator H16 (CnFadB), our study provides insights into fatty acid metabolism in this bacterium. Unlike other known enzymes, CnFadB functions as a monomer and the non-sequential action of FadA and FadB appears to impact PHA synthesis/degradation.
Cupriavidus necator H16 is a gram-negative chemolithoautotrophic bacterium that has been extensively studied for biosynthesis and biodegradation of polyhydroxyalkanoate (PHA) plastics. To improve our understanding of fatty acid metabolism for PHA production, we determined the crystal structure of multi-functional enoyl-CoA hydratase from Cupriavidus necator H16 (CnFadB). The predicted model of CnFadB created by AlphaFold was used to solve the phase problem during determination of the crystal structure of the protein. The CnFadB structure consists of two distinctive domains, an N-terminal enol-CoA hydratase (ECH) domain and a C-terminal 3-hydroxyacyl-CoA dehydrogenase (HAD) domain, and the substrate-and cofactor-binding modes of these two functional domains were identified. Unlike other known FadB enzymes that exist as dimers complexed with FadA, CnFadB functions as a monomer without forming a complex with CnFadA. Small angle X-ray scattering (SAXS) measurement further proved that CnFadB exists as a monomer in solution. The non-sequential action of FadA and FadB in C. necator appears to affect 8-oxidation and PHA synthesis/degradation.
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