7TVW
Crystal structure of Arabidopsis thaliana DLK2
Summary for 7TVW
| Entry DOI | 10.2210/pdb7tvw/pdb |
| Descriptor | Alpha/beta-Hydrolases superfamily protein (2 entities in total) |
| Functional Keywords | sesquiterpene lactone perception, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 30207.77 |
| Authors | Burger, M.,Chory, J. (deposition date: 2022-02-06, release date: 2022-09-28, Last modification date: 2023-10-18) |
| Primary citation | Burger, M.,Honda, K.,Kondoh, Y.,Hong, S.,Watanabe, N.,Osada, H.,Chory, J. Crystal structure of Arabidopsis DWARF14-LIKE2 (DLK2) reveals a distinct substrate binding pocket architecture. Plant Direct, 6:e446-e446, 2022 Cited by PubMed Abstract: In , 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. PubMed: 36172078DOI: 10.1002/pld3.446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.48 Å) |
Structure validation
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