6SW2
Crystal Structure of P. aeruginosa PqsL in complex with 2-aminobenzoylacetate
Summary for 6SW2
| Entry DOI | 10.2210/pdb6sw2/pdb |
| Descriptor | Probable FAD-dependent monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, 3-(2-aminophenyl)-3-oxopropanoic acid, ... (8 entities in total) |
| Functional Keywords | oxidoreductase, photocatalysis, fad, nad(p), biosynthetic pathway, antibiotic |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 46115.84 |
| Authors | Mattevi, A.,Rovida, S. (deposition date: 2019-09-19, release date: 2020-06-03, Last modification date: 2024-10-23) |
| Primary citation | Ernst, S.,Rovida, S.,Mattevi, A.,Fetzner, S.,Drees, S.L. Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer. Nat Commun, 11:2600-2600, 2020 Cited by PubMed Abstract: 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. PubMed: 32451409DOI: 10.1038/s41467-020-16450-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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