5ncc | pdb_00005ncc

Structure of Fatty acid Photodecarboxylase in complex with FAD and palmitic acid

spinqualitylabelsall models 5ncc, resolution 3.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ncc is a 6 chain structure with sequence from Chlva. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Although many organisms capture or respond to sunlight, few enzymes are known to be driven by light. Among these are DNA photolyases and the photosynthetic reaction centers. Here, we show that the microalga Chlorella variabilis NC64A harbors a photoenzyme that acts in lipid metabolism. This enzyme belongs to an algae-specific clade of the glucose-methanol-choline oxidoreductase family and catalyzes the decarboxylation of free fatty acids to n-alkanes or -alkenes in response to blue light. Crystal structure of the protein reveals a fatty acid-binding site in a hydrophobic tunnel leading to the light-capturing flavin adenine dinucleotide (FAD) cofactor. The decarboxylation is initiated through electron abstraction from the fatty acid by the photoexcited FAD with a quantum yield >80%. This photoenzyme, which we name fatty acid photodecarboxylase, may be useful in light-driven, bio-based production of hydrocarbons. An algal photoenzyme converts fatty acids to hydrocarbons.,Sorigue D, Legeret B, Cuine S, Blangy S, Moulin S, Billon E, Richaud P, Brugiere S, Coute Y, Nurizzo D, Muller P, Brettel K, Pignol D, Arnoux P, Li-Beisson Y, Peltier G, Beisson F Science. 2017 Sep 1;357(6354):903-907. doi: 10.1126/science.aan6349. PMID:28860382 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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