7O0T
Crystal structure of Chloroflexus aggregans ene-reductase CaOYE holoenzyme
Summary for 7O0T
| Entry DOI | 10.2210/pdb7o0t/pdb |
| Descriptor | NADH:flavin oxidoreductase/NADH oxidase, FLAVIN MONONUCLEOTIDE, MALONATE ION, ... (4 entities in total) |
| Functional Keywords | ene-reductase, fmn-binding protein, old yellow enzyme, oxidoreductase |
| Biological source | Chloroflexus aggregans (strain MD-66 / DSM 9485) |
| Total number of polymer chains | 4 |
| Total formula weight | 153508.11 |
| Authors | Robescu, M.S.,Niero, M.,Loprete, G.,Bergantino, E.,Cendron, L. (deposition date: 2021-03-26, release date: 2021-05-05, Last modification date: 2024-01-31) |
| Primary citation | Robescu, M.S.,Niero, M.,Loprete, G.,Cendron, L.,Bergantino, E. A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans . Microorganisms, 9:-, 2021 Cited by PubMed Abstract: Aiming at expanding the biocatalytic toolbox of ene-reductase enzymes, we decided to explore photosynthetic extremophile microorganisms as unique reservoir of (new) biocatalytic activities. We selected a new thermophilic ene-reductase homologue in , a peculiar filamentous bacterium. We report here on the functional and structural characterization of this new enzyme, which we called OYE. Produced in high yields in recombinant form, it proved to be a robust biocatalyst showing high thermostability, good solvent tolerance and a wide range of pH optimum. In a preliminary screening, OYE displayed a restricted substrate spectrum (with generally lower activities compared to other ene-reductases); however, given the amazing metabolic ductility and versatility of , further investigations could pinpoint peculiar chemical activities. X-ray crystal structure has been determined, revealing conserved features of Class III (or thermophilic-like group) of the family of Old Yellow Enzymes: in the crystal packing, the enzyme was found to assemble as dimer even if it behaves as a monomer in solution. The description of OYE catalytic properties and crystal structure provides new details useful for enlarging knowledge, development and application of this class of enzymes. PubMed: 33925162DOI: 10.3390/microorganisms9050953 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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