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Cell Rep. 2019 Jan 22;26(4):855-865.e5. doi: 10.1016/j.celrep.2019.01.003.

Structural Basis of Karrikin and Non-natural Strigolactone Perception in Physcomitrella patens.

Author information

1
Plant Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.
2
Graduate School of Life Sciences, Tōhoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan.
3
Graduate School of Life Sciences, Tōhoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan; School of Agriculture, Meiji University, 1-1-1, Higashi-mita, Tama-ku, Kawasaki 214-8571, Japan.
4
Graduate School of Life Sciences, Tōhoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan; Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. Electronic address: shinjiro@scl.kyoto-u.ac.jp.
5
Plant Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA; Howard Hughes Medical Institute, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: chory@salk.edu.

Abstract

In plants, strigolactones are perceived by the dual receptor-hydrolase DWARF14 (D14). D14 belongs to the superfamily of α/β 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 KAR1 and the non-natural strigolactone isomer (-)-5-deoxystrigol in a highly stereoselective manner.

KEYWORDS:

Physcomitrella patens; karrikin; strigolactone; α/β hydrolases

PMID:
30673608
DOI:
10.1016/j.celrep.2019.01.003
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