7o0t

Crystal structure of Chloroflexus aggregans ene-reductase CaOYE holoenzyme

spinqualitylabelsall models 7o0t, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7o0t is a 4 chain structure with sequence from Chloroflexus aggregans DSM 9485. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FMN, MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B8G5D6_CHLAD Publication Abstract from PubMed 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 Chloroflexus aggregans, a peculiar filamentous bacterium. We report here on the functional and structural characterization of this new enzyme, which we called CaOYE. 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, CaOYE displayed a restricted substrate spectrum (with generally lower activities compared to other ene-reductases); however, given the amazing metabolic ductility and versatility of Chloroflexus aggregans, 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 CaOYE catalytic properties and crystal structure provides new details useful for enlarging knowledge, development and application of this class of enzymes. A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic Bacterium Chloroflexus aggregans.,Robescu MS, Niero M, Loprete G, Cendron L, Bergantino E Microorganisms. 2021 Apr 28;9(5). pii: microorganisms9050953. doi:, 10.3390/microorganisms9050953. PMID:33925162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NADPH dehydrogenase

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