期刊
SCIENCE
卷 336, 期 6089, 页码 1708-1711出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1221863
关键词
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资金
- NSF [MCB-1157771]
- U.S. Department of Agriculture-National Institute of Food and Agriculture [MOW-2010-05240]
- American Society of Plant Biologists
- Howard Hughes Medical Institute-Washington University
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1157771] Funding Source: National Science Foundation
Acyl acid amido synthetases of the GH3 family act as critical prereceptor modulators of plant hormone action; however, the molecular basis for their hormone selectivity is unclear. Here, we report the crystal structures of benzoate-specific Arabidopsis thaliana AtGH3.12/PBS3 and jasmonic acid-specific AtGH3.11/JAR1. These structures, combined with biochemical analysis, define features for the conjugation of amino acids to diverse acyl acid substrates and highlight the importance of conformational changes in the carboxyl-terminal domain for catalysis. We also identify residues forming the acyl acid binding site across the GH3 family and residues critical for amino acid recognition. Our results demonstrate how a highly adaptable three-dimensional scaffold is used for the evolution of promiscuous activity across an enzyme family for modulation of plant signaling molecules.
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