Title : Crystal structure of Arabidopsis DWARF14-LIKE2 (DLK2) reveals a distinct substrate binding pocket architecture - Burger_2022_Plant.Direct_6_e466 |
Author(s) : Burger M , Honda K , Kondoh Y , Hong S , Watanabe N , Osada H , Chory J |
Ref : Plant Direct , 6 :e446 , 2022 |
Abstract :
In Arabidopsis thaliana, the Sigma factor B regulator RsbQ-like family of alpha/beta 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 A 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. |
PubMedSearch : Burger_2022_Plant.Direct_6_e466 |
PubMedID: 36172078 |
Gene_locus related to this paper: arath-Q9LK01 |
Gene_locus | arath-Q9LK01 |
Structure | 7TVW |
Burger M, Honda K, Kondoh Y, Hong S, Watanabe N, Osada H, Chory J (2022)
Crystal structure of Arabidopsis DWARF14-LIKE2 (DLK2) reveals a distinct substrate binding pocket architecture
Plant Direct
6 :e446
Burger M, Honda K, Kondoh Y, Hong S, Watanabe N, Osada H, Chory J (2022)
Plant Direct
6 :e446