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• W2026863047 abstract "Control over phenoxy radical-radical coupling reactions in vivo in vascular plants was enigmatic until our discovery of dirigent proteins (DPs, from the Latin dirigere, to guide or align). The first three-dimensional structure of a DP ((+)-pinoresinol-forming DP, 1.95 Å resolution, rhombohedral space group H32)) is reported herein. It has a tightly packed trimeric structure with an eight-stranded β-barrel topology for each DP monomer. Each putative substrate binding and orientation coupling site is located on the trimer surface but too far apart for intermolecular coupling between sites. It is proposed that each site enables stereoselective coupling (using either two coniferyl alcohol radicals or a radical and a monolignol). Interestingly, there are six differentially conserved residues in DPs affording either the (+)- or (−)-antipodes in the vicinity of the putative binding site and region known to control stereoselectivity. DPs are involved in lignan biosynthesis, whereas dirigent domains/sites have been implicated in lignin deposition.BackgroundDirigent protein (DP) discovery gave new paradigm for monolignol-derived coupling in planta.Results(+)-Pinoresinol-forming DP (PsDRR206) three-dimensional structure was obtained at 1.95 Å resolution.ConclusionThe tightly packed trimeric DP has three putative substrate binding sites spatially far apart, suggesting that each site involves monomer coupling directly.SignificanceNew insights into monolignol radical-radical coupling in planta. Control over phenoxy radical-radical coupling reactions in vivo in vascular plants was enigmatic until our discovery of dirigent proteins (DPs, from the Latin dirigere, to guide or align). The first three-dimensional structure of a DP ((+)-pinoresinol-forming DP, 1.95 Å resolution, rhombohedral space group H32)) is reported herein. It has a tightly packed trimeric structure with an eight-stranded β-barrel topology for each DP monomer. Each putative substrate binding and orientation coupling site is located on the trimer surface but too far apart for intermolecular coupling between sites. It is proposed that each site enables stereoselective coupling (using either two coniferyl alcohol radicals or a radical and a monolignol). Interestingly, there are six differentially conserved residues in DPs affording either the (+)- or (−)-antipodes in the vicinity of the putative binding site and region known to control stereoselectivity. DPs are involved in lignan biosynthesis, whereas dirigent domains/sites have been implicated in lignin deposition. Dirigent protein (DP) discovery gave new paradigm for monolignol-derived coupling in planta. (+)-Pinoresinol-forming DP (PsDRR206) three-dimensional structure was obtained at 1.95 Å resolution. The tightly packed trimeric DP has three putative substrate binding sites spatially far apart, suggesting that each site involves monomer coupling directly." @default.
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• W2026863047 date "2015-01-01" @default.
• W2026863047 modified "2023-10-16" @default.
• W2026863047 title "Trimeric Structure of (+)-Pinoresinol-forming Dirigent Protein at 1.95 Å Resolution with Three Isolated Active Sites" @default.
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• W2026863047 doi "https://doi.org/10.1074/jbc.m114.611780" @default.
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