Crystal Structure of DWARF14-LIKE2 (DLK2) Reveals a Distinct Substrate Binding Pocket Architecture

Overview

Journal Plant Direct

Specialty Biology

Date 2022 Sep 29

PMID 36172078

Authors

Marco Burger

Kaori Honda

Yasumitsu Kondoh

Sharon Hong

Nobumoto Watanabe

Hiroyuki Osada

Joanne Chory

Affiliations

Soon will be listed here.

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.

Citing Articles

Karrikin signalling: impacts on plant development and abiotic stress tolerance.

Kamran M, Melville K, Waters M J Exp Bot. 2023; 75(4):1174-1186.

PMID: 38001035 PMC: 10860534. DOI: 10.1093/jxb/erad476.

Crystal structure of DWARF14-LIKE2 (DLK2) reveals a distinct substrate binding pocket architecture.

Burger M, Honda K, Kondoh Y, Hong S, Watanabe N, Osada H Plant Direct. 2022; 6(9):e446.

PMID: 36172078 PMC: 9470386. DOI: 10.1002/pld3.446.

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