8R2U
Crystal structure of hydroquinone-2-hydroxylase from Trametes versicolor (TvMNX3)
Summary for 8R2U
| Entry DOI | 10.2210/pdb8r2u/pdb |
| Descriptor | Phenol 2-monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | fungi, hydroquinone, hydroxylase, oxidoreductase |
| Biological source | Trametes versicolor |
| Total number of polymer chains | 4 |
| Total formula weight | 278989.51 |
| Authors | Zahn, M.,Kuatsjah, E.,Salvachua, D. (deposition date: 2023-11-07, release date: 2024-11-13, Last modification date: 2024-12-04) |
| Primary citation | Kuatsjah, E.,Schwartz, A.,Zahn, M.,Tornesakis, K.,Kellermyer, Z.A.,Ingraham, M.A.,Woodworth, S.P.,Ramirez, K.J.,Cox, P.A.,Pickford, A.R.,Salvachua, D. Biochemical and structural characterization of enzymes in the 4-hydroxybenzoate catabolic pathway of lignin-degrading white-rot fungi. Cell Rep, 43:115002-115002, 2024 Cited by PubMed Abstract: White-rot fungi (WRF) are the most efficient lignin-degrading organisms in nature. However, their capacity to use lignin-related aromatic compounds, such as 4-hydroxybenzoate, as carbon sources has only been described recently. Previously, the hydroxyquinol pathway was proposed for the bioconversion of these compounds in fungi, but gene- and structure-function relationships of the full enzymatic pathway remain uncharacterized in any single fungal species. Here, we characterize seven enzymes from two WRF, Trametes versicolor and Gelatoporia subvermispora, which constitute a four-enzyme cascade from 4-hydroxybenzoate to β-ketoadipate via the hydroxyquinol pathway. Furthermore, we solve the crystal structure of four of these enzymes and identify mechanistic differences with the closest bacterial and fungal structural homologs. Overall, this research expands our understanding of aromatic catabolism by WRF and establishes an alternative strategy for the conversion of lignin-related compounds to the valuable molecule β-ketoadipate, contributing to the development of biological processes for lignin valorization. PubMed: 39589922DOI: 10.1016/j.celrep.2024.115002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
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