6sw1 | pdb_00006sw1

Crystal Structure of P. aeruginosa PqsL: R41Y, I43R, G45R, C105G mutant

spinqualitylabelsall models 6sw1, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6sw1 is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: FAD, GOL, PEG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HWJ1_PSEAE Publication Abstract from PubMed Light-dependent or light-stimulated catalysis provides a multitude of perspectives for implementation in technological or biomedical applications. Despite substantial progress made in the field of photobiocatalysis, the number of usable light-responsive enzymes is still very limited. Flavoproteins have exceptional potential for photocatalytic applications because the name-giving cofactor intrinsically features light-dependent reactivity, undergoing photoreduction with a variety of organic electron donors. However, in the vast majority of these enzymes, photoreactivity of the enzyme-bound flavin is limited or even suppressed. Here, we present a flavoprotein monooxygenase in which catalytic activity is controllable by blue light illumination. The reaction depends on the presence of nicotinamide nucleotide-type electron donors, which do not support the reaction in the absence of light. Employing various experimental approaches, we demonstrate that catalysis depends on a protein-mediated photoreduction of the flavin cofactor, which proceeds via a radical mechanism and a transient semiquinone intermediate. Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer.,Ernst S, Rovida S, Mattevi A, Fetzner S, Drees SL Nat Commun. 2020 May 25;11(1):2600. doi: 10.1038/s41467-020-16450-y. PMID:32451409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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