8AEO
Malonyl-CoA reductase from Chloroflexus aurantiacus - C-terminal R773A variant
Summary for 8AEO
| Entry DOI | 10.2210/pdb8aeo/pdb |
| Related | 8A30 8A7S 8A8T |
| Descriptor | Short-chain dehydrogenase/reductase SDR, SULFATE ION (3 entities in total) |
| Functional Keywords | rossmann fold, site-directed mutagenesis, bi-functional enzyme, reductase, malonyl-coa, 3-hydroxypropionate, 3-hp cycle, oxidoreductase |
| Biological source | Chloroflexus aurantiacus J-10-fl |
| Total number of polymer chains | 1 |
| Total formula weight | 73619.60 |
| Authors | Kabasakal, B.V.,Murray, J.W. (deposition date: 2022-07-13, release date: 2023-04-05, Last modification date: 2024-02-07) |
| Primary citation | Kabasakal, B.V.,Cotton, C.A.R.,Murray, J.W. Dynamic lid domain of Chloroflexus aurantiacus Malonyl-CoA reductase controls the reaction. Biochimie, 219:12-20, 2023 Cited by PubMed Abstract: Malonyl-Coenzyme A Reductase (MCR) in Chloroflexus aurantiacus, a characteristic enzyme of the 3-hydroxypropionate (3-HP) cycle, catalyses the reduction of malonyl-CoA to 3-HP. MCR is a bi-functional enzyme; in the first step, malonyl-CoA is reduced to the free intermediate malonate semialdehyde by the C-terminal region of MCR, and this is further reduced to 3-HP by the N-terminal region of MCR. Here we present the crystal structures of both N-terminal and C-terminal regions of the MCR from C. aurantiacus. A catalytic mechanism is suggested by ligand and substrate bound structures, and structural and kinetic studies of MCR variants. Both MCR structures reveal one catalytic, and one non-catalytic SDR (short chain dehydrogenase/reductase) domain. C-terminal MCR has a lid domain which undergoes a conformational change and controls the reaction. In the proposed mechanism of the C-terminal MCR, the conversion of malonyl-CoA to malonate semialdehyde is based on the reduction of malonyl-CoA by NADPH, followed by the decomposition of the hemithioacetal to produce malonate semialdehyde and coenzyme A. Conserved arginines, Arg734 and Arg773 are proposed to play key roles in the mechanism and conserved Ser719, and Tyr737 are other essential residues forming an oxyanion hole for the substrate intermediates. PubMed: 37952891DOI: 10.1016/j.biochi.2023.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
Download full validation report
