期刊
CELL REPORTS
卷 26, 期 4, 页码 855-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2019.01.003
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资金
- NIH, National Institute of General Medical Sciences
- Howard Hughes Medical Institute
- Office of Science, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-AC02-05CH11231]
- Mass Spectrometry Core of the Salk Institute
- NIH-NCI CCSG [P30 014195]
- Helmsley Center for Genomic Medicine
In plants, strigolactones are perceived by the dual receptor-hydrolase DWARF14 (D14). D14 belongs to the superfamily of alpha/beta hydrolases and is structurally similar to the karrikin receptor KARRIKIN INSENSITIVE 2 (KAI2). The moss Physcomitrella patens is an ideal model system for studying this receptor family, because it includes 11 highly related family members with unknown ligand specificity. We present the crystal structures of three Physcomitrella D14/KAI2-like proteins and describe a loop-based mechanism that leads to a permanent widening of the hydrophobic substrate gorge. We have identified protein clades that specifically perceive the karrikin KAR(1) and the non-natural strigolactone isomer (similar to)-5-deoxystrigol in a highly stereoselective manner.
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