5lte

Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM)

spinqualitylabelsall models 5lte, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lte is a 1 chain structure with sequence from Pseudomonas mendocina ymp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: ETX, HEM, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4XXY9_PSEMY Publication Abstract from PubMed The universal Per-ARNT-Sim (PAS) domain functions as a signal transduction module involved in sensing diverse stimuli such as small molecules, light, redox state and gases. The highly evolvable PAS scaffold can bind a broad range of ligands, including haem, flavins and metal ions. However, although these ligands can support catalytic activity, to our knowledge no enzymatic PAS domain has been found. Here we report characterization of the first PAS enzyme: a haem-dependent oxidative N-demethylase. Unrelated to other amine oxidases, this enzyme contains haem, flavin mononucleotide, 2Fe-2S and tetrahydrofolic acid cofactors, and specifically catalyses the NADPH-dependent oxidation of dimethylamine. The structure of the alpha subunit reveals that it is a haem-binding PAS domain, similar in structure to PAS gas sensors. The dimethylamine substrate forms part of a highly polarized oxygen-binding site, and directly assists oxygen activation by acting as both an electron and proton donor. Our data reveal that the ubiquitous PAS domain can make the transition from sensor to enzyme, suggesting that the PAS scaffold can support the development of artificial enzymes. An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.,Ortmayer M, Lafite P, Menon BR, Tralau T, Fisher K, Denkhaus L, Scrutton NS, Rigby SE, Munro AW, Hay S, Leys D Nature. 2016 Nov 24;539(7630):593-597. doi: 10.1038/nature20159. Epub 2016 Nov, 16. PMID:27851736 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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