5OMU
Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with syringol
Summary for 5OMU
| Entry DOI | 10.2210/pdb5omu/pdb |
| Descriptor | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, 2,6-dimethoxyphenol, ... (4 entities in total) |
| Functional Keywords | cytochrome, p450, guaiacol, lignin, cyp255a, amycolatopsis, heme, haem, oxidoreductase, syringol |
| Biological source | Amycolatopsis sp. ATCC 39116 |
| Total number of polymer chains | 1 |
| Total formula weight | 46223.42 |
| Authors | Mallinson, S.J.B.,Johnson, C.W.,Neidle, E.L.,Beckham, G.T.,McGeehan, J.E. (deposition date: 2017-08-01, release date: 2018-07-04, Last modification date: 2024-06-19) |
| Primary citation | Mallinson, S.J.B.,Machovina, M.M.,Silveira, R.L.,Garcia-Borras, M.,Gallup, N.,Johnson, C.W.,Allen, M.D.,Skaf, M.S.,Crowley, M.F.,Neidle, E.L.,Houk, K.N.,Beckham, G.T.,DuBois, J.L.,McGeehan, J.E. A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion. Nat Commun, 9:2487-2487, 2018 Cited by PubMed Abstract: 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. PubMed: 29950589DOI: 10.1038/s41467-018-04878-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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