Open AccessCrystal structure of Arabidopsis DWARF14‐LIKE2 (DLK2) reveals a distinct substrate binding pocket architecture
Author(s) -
Bürger Marco,
Honda Kaori,
Kondoh Yasumitsu,
Hong Sharon,
Watanabe Nobumoto,
Osada Hiroyuki,
Chory Joanne
Publication year - 2022
Publication title -
plant direct
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.211
H-Index - 11
ISSN - 2475-4455
DOI - 10.1002/pld3.446
Subject(s) - arabidopsis , residue (chemistry) , chemistry , binding site , ligand (biochemistry) , receptor , biophysics , stereochemistry , microbiology and biotechnology , biochemistry , biology , mutant , gene
Abstract In Arabidopsis thaliana , the Sigma factor B regulator RsbQ‐like family of α/β hydrolases contains the strigolactone (SL) receptor DWARF14 (AtD14), the karrikin receptor KARRIKIN INSENSITIVE2 (AtKAI2), and DWARF14‐LIKE2 (AtDLK2), a protein of unknown function. Despite very similar protein folds, AtD14 and AtKAI2 differ in size and architecture of their ligand binding pockets, influencing their substrate specificity. We present the 1.5 Å crystal structure of AtDLK2, revealing the smallest ligand binding pocket in the protein family, bordered by two unique glycine residues. We identified a gatekeeper residue in the protein's lid domain and present a pyrrolo‐quinoline‐dione compound that inhibits AtDLK2's enzymatic activity.