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TitleCryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity.
Journal, issue, pagesInt J Biol Macromol, Vol. 242, Issue Pt 1, Page 124676, Year 2023
Publish dateJul 1, 2023
AuthorsJae-Woo Ahn / Sangwoo Kim / Jiyeon Hong / Kyung-Jin Kim /
PubMed AbstractThe platform chemical 3-hydroxypropionic acid is used to synthesize various valuable materials, including bioplastics. Bifunctional malonyl-CoA reductase is a key enzyme in 3-hydroxypropionic acid ...The platform chemical 3-hydroxypropionic acid is used to synthesize various valuable materials, including bioplastics. Bifunctional malonyl-CoA reductase is a key enzyme in 3-hydroxypropionic acid biosynthesis as it catalyzes the two-step reduction of malonyl-CoA to malonate semialdehyde to 3-hydroxypropionic acid. Here, we report the cryo-EM structure of a full-length malonyl-CoA reductase protein from Chloroflexus aurantiacus (CaMCR). The EM model of CaMCR reveals a tandem helix architecture comprising an N-terminal (CaMCR) and a C-terminal (CaMCR) domain. The CaMCR model also revealed that the enzyme undergoes a dynamic domain movement between CaMCR and CaMCR due to the presence of a flexible linker between these two domains. Increasing the flexibility and extension of the linker resulted in a twofold increase in enzyme activity, indicating that for CaMCR, domain movement is crucial for high enzyme activity. We also describe the structural features of CaMCR and CaMCR. This study reveals the protein structures underlying the molecular mechanism of CaMCR and thereby provides valuable information for future enzyme engineering to improve the productivity of 3-hydroxypropionic acid.
External linksInt J Biol Macromol / PubMed:37146856
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 4.1 Å
Structure data

34840

8hjw

EMDB-34840, PDB-8hjw:
Bi-functional malonyl-CoA reductuase from Chloroflexus aurantiacus
Method: EM (single particle) / Resolution: 4.1 Å

PDB-8i6z:
Crystal structure of apo-form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-8i70:
Crystal structure of NADP-binding form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-TLA:
L(+)-TARTARIC ACID

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Source
  • chloroflexus aurantiacus (bacteria)
KeywordsOXIDOREDUCTASE / malonyl-CoA reductase (MCR) / bi-functional enzyme / NADPH-dependent reduction / NAD(P)-binding protein / Short-chain reductase

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