6K8W

Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase

Summary for 6K8W

• Entry DOI: 10.2210/pdb6k8w/pdb
• Descriptor: NAD-dependent epimerase/dehydratase:Short-chain dehydrogenase/reductase SDR, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: sdr domain, oxidoreductase
• Biological source: Porphyrobacter dokdonensis DSW-74
• Total number of polymer chains: 2
• Total formula weight: 124121.47

Authors

Kim, S.,Kim, K.-J. (deposition date: 2019-06-13, release date: 2020-03-18, Last modification date: 2023-11-22)

Primary citation

Son, H.F.,Kim, S.,Seo, H.,Hong, J.,Lee, D.,Jin, K.S.,Park, S.,Kim, K.J.
Structural insight into bi-functional malonyl-CoA reductase.
Environ.Microbiol., 22:752-765, 2020

PubMed Abstract: The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme.

PubMed: 31814251
DOI: 10.1111/1462-2920.14885

Experimental method

X-RAY DIFFRACTION (3.17 Å)