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

Marco Bürger | Zendy; Kiyoshi Mashiguchi | Zendy; Hyun Jee Lee | Zendy; Misaki Nakano | Zendy; Kodai Takemoto | Zendy; Yoshiya Seto | Zendy; Shinjiro Yamaguchi | Zendy; Joanne Chory | Zendy

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

Author(s) -

Marco Bürger,

Kiyoshi Mashiguchi,

Hyun Jee Lee,

Misaki Nakano,

Kodai Takemoto,

Yoshiya Seto,

Shinjiro Yamaguchi,

Joanne Chory

Publication year - 2019

Publication title -

cell reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.264

H-Index - 154

eISSN - 2639-1856

pISSN - 2211-1247

DOI - 10.1016/j.celrep.2019.01.003

Subject(s) - physcomitrella patens , strigolactone , bryopsida , hydrolase , biology , moss , microbiology and biotechnology , chemistry , genetics , botany , biochemistry , enzyme , gene , mutant , arabidopsis

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 KAR 1 and the non-natural strigolactone isomer (-)-5-deoxystrigol in a highly stereoselective manner.

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