6UH9

Crystal structure of DAD2 D166A mutant

Summary for 6UH9

• Entry DOI: 10.2210/pdb6uh9/pdb
• Descriptor: Decreased Apical Dominance 2, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: strigolactone receptor, dad2, hydrolase
• Biological source: Petunia hybrida (Petunia)
• Total number of polymer chains: 2
• Total formula weight: 59878.53

Authors

Sharma, P.,Hamiaux, C.,Snowden, K.C. (deposition date: 2019-09-27, release date: 2020-02-26, Last modification date: 2023-10-11)

Primary citation

Lee, H.W.,Sharma, P.,Janssen, B.J.,Drummond, R.S.M.,Luo, Z.,Hamiaux, C.,Collier, T.,Allison, J.R.,Newcomb, R.D.,Snowden, K.C.
Flexibility of the petunia strigolactone receptor DAD2 promotes its interaction with signaling partners.
J.Biol.Chem., 295:4181-4193, 2020

PubMed Abstract: Strigolactones (SLs) are terpenoid-derived plant hormones that regulate various developmental processes, particularly shoot branching, root development, and leaf senescence. The SL receptor has an unusual mode of action. Upon binding SL, it hydrolyzes the hormone, and then covalently binds one of the hydrolytic products. These initial events enable the SL receptor DAD2 (in petunia) to interact with the F-box protein PhMAX2A of the Skp-Cullin-F-box (SCF) complex and/or a repressor of SL signaling, PhD53A. However, it remains unclear how binding and hydrolysis structurally alters the SL receptor to enable its engagement with signaling partners. Here, we used mutagenesis to alter DAD2 and affect SL hydrolysis or DAD2's ability to interact with its signaling partners. We identified three DAD2 variants whose hydrolytic activity had been separated from the receptor's interactions with PhMAX2A or PhD53A. Two variants, DAD2 and DAD2, having substitutions in the core α/β hydrolase-fold domain and the hairpin, exhibited hormone-independent interactions with PhMAX2A and PhD53A, respectively. Conversely, the DAD2 variant could not interact with PhMAX2A in the presence of SL, but its interaction with PhD53A remained unaffected. Structural analyses of DAD2 and DAD2 revealed only small differences compared with the structure of the WT receptor. Results of molecular dynamics simulations of the DAD2 structure suggested that increased flexibility is a likely cause for its SL-independent interaction with PhMAX2A. Our results suggest that PhMAX2A and PhD53A have distinct binding sites on the SL receptor and that its flexibility is a major determinant of its interactions with these two downstream regulators.

PubMed: 32071083
DOI: 10.1074/jbc.RA119.011509

Experimental method

X-RAY DIFFRACTION (1.52 Å)