Crystal structure of multi-functional enzyme FadB from Cupriavidus necator: Non-formation of FadAB complex.
Arch Biochem Biophys
; 730: 109391, 2022 11 15.
Article
em En
| MEDLINE
| ID: mdl-36087768
ABSTRACT
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 ß-oxidation and PHA synthesis/degradation.
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Bases de dados:
MEDLINE
Assunto principal:
Cupriavidus necator
/
Poli-Hidroxialcanoatos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
2022
Tipo de documento:
Article