8R2X

Crystal structure of hydroxyquinol-1,2-dioxygenase from Rhodococcus jostii RHA1 (RjTsdC)

8R2X の概要

• エントリーDOI: 10.2210/pdb8r2x/pdb
• 分子名称: 6-chlorohydroxyquinol-1,2-dioxygenase, PHOSPHATIDYLETHANOLAMINE, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: fungi, hydroxyquinol, 1, 2-dioxygenase, oxidoreductase
• 由来する生物種: Rhodococcus jostii RHA1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68219.56

構造登録者

Zahn, M.,Kuatsjah, E.,Salvachua, D. (登録日: 2023-11-07, 公開日: 2024-11-13, 最終更新日: 2024-12-04)

主引用文献

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

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: 39589922
DOI: 10.1016/j.celrep.2024.115002

実験手法

X-RAY DIFFRACTION (1.573 Å)