5omr | pdb_00005omr

Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with vanillin.

spinqualitylabelsall models 5omr, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5omr is a 1 chain structure with sequence from Amycolatopsis sp. ATCC 39116. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.68Å Ligands: HEM, V55 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A3B6UEE9_AMYS7 Publication Abstract from PubMed Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-derived aromatic compounds, and is often a key bottleneck for both native and engineered bioconversion pathways. Here, we report the comprehensive characterization of a promiscuous P450 aryl-O-demethylase, consisting of a cytochrome P450 protein from the family CYP255A (GcoA) and a three-domain reductase (GcoB) that together represent a new two-component P450 class. Though originally described as converting guaiacol to catechol, we show that this system efficiently demethylates both guaiacol and an unexpectedly wide variety of lignin-relevant monomers. Structural, biochemical, and computational studies of this novel two-component system elucidate the mechanism of its broad substrate specificity, presenting it as a new tool for a critical step in biological lignin conversion. A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion.,Mallinson SJB, Machovina MM, Silveira RL, Garcia-Borras M, Gallup N, Johnson CW, Allen MD, Skaf MS, Crowley MF, Neidle EL, Houk KN, Beckham GT, DuBois JL, McGeehan JE Nat Commun. 2018 Jun 27;9(1):2487. doi: 10.1038/s41467-018-04878-2. PMID:29950589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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