Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 290, Issue 3, Pages 1308-1318Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.611780
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Funding
- U.S. Dept. of Energy, Office of Science, Basic Energy Sciences (BES) [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research (BER)
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
- Dept. of Energy's BER
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1052557] Funding Source: National Science Foundation
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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 angstrom resolution, rhombohedral space group H32)) is reported herein. It has a tightly packed trimeric structure with an eight-stranded beta-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.
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