| Autor: |
Marco Bürger, Kaori Honda, Yasumitsu Kondoh, Sharon Hong, Nobumoto Watanabe, Hiroyuki Osada, Joanne Chory |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Plant Direct, Vol 6, Iss 9, Pp n/a-n/a (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2475-4455 |
| DOI: |
10.1002/pld3.446 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
Plný text