6uh8 | pdb_00006uh8

Crystal structure of DAD2 N242I mutant

spinqualitylabelsall models 6uh8, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6uh8 is a 2 chain structure with sequence from Pethy. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, MES, MG, SO4 Gene: dad2 (PETHY) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 hydrolyses 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(N242I) and DAD2(F135A), having substitutions in the core alpha/beta hydrolase fold domain and the hairpin, exhibited hormone-independent interactions with PhMAX2A and PhD53A respectively. Conversely, the DAD2(D166A) variant could not interact with PhMAX2A in the presence of SL, but its interaction with PhD53A remained unaffected. Structural analyses of DAD2N242I and DAD2D166A revealed only small differences compared with the structure of the wild-type receptor. Results of molecular dynamics simulations of the DAD2(N242I) 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. Flexibility of the petunia strigolactone receptor DAD2 promotes its interaction with signaling partners.,Lee HW, Sharma P, Janssen BJ, Drummond RSM, Luo Z, Hamiaux C, Collier T, Allison JR, Newcomb RD, Snowden KC J Biol Chem. 2020 Feb 17. pii: RA119.011509. doi: 10.1074/jbc.RA119.011509. PMID:32071083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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