9J6I
Crystal structure of the ABA receptor PYL1 in complex with DBSA compound
Summary for 9J6I
Entry DOI | 10.2210/pdb9j6i/pdb |
Descriptor | Abscisic acid receptor PYL1, 5-bromanyl-N2-[(4-bromophenyl)-bis(oxidanyl)-$l^4-sulfanyl]-N1,N1,N3,N3-tetrakis(oxidanyl)benzene-1,2,3-triamine (3 entities in total) |
Functional Keywords | aba receptor, pyl1, lipid binding protein |
Biological source | Arabidopsis thaliana (thale cress) |
Total number of polymer chains | 2 |
Total formula weight | 41040.51 |
Authors | |
Primary citation | Wang, Z.Z.,Cao, M.J.,Yan, J.,Dong, J.,Chen, M.X.,Yang, J.F.,Li, J.H.,Ying, R.N.,Gao, Y.Y.,Li, L.,Leng, Y.N.,Tian, Y.,Hewage, K.A.H.,Pei, R.J.,Huang, Z.Y.,Yin, P.,Zhu, J.K.,Hao, G.F.,Yang, G.F. Stabilization of dimeric PYR/PYL/RCAR family members relieves abscisic acid-induced inhibition of seed germination. Nat Commun, 15:8077-8077, 2024 Cited by PubMed Abstract: Abscisic acid (ABA) is the primary preventing factor of seed germination, which is crucial to plant survival and propagation. ABA-induced seed germination inhibition is mainly mediated by the dimeric PYR/PYL/RCAR (PYLs) family members. However, little is known about the relevance between dimeric stability of PYLs and seed germination. Here, we reveal that stabilization of PYL dimer can relieve ABA-induced inhibition of seed germination using chemical genetic approaches. Di-nitrobensulfamide (DBSA), a computationally designed chemical probe, yields around ten-fold improvement in receptor affinity relative to ABA. DBSA reverses ABA-induced inhibition of seed germination mainly through dimeric receptors and recovers the expression of ABA-responsive genes. DBSA maintains PYR1 in dimeric state during protein oligomeric state experiment. X-ray crystallography shows that DBSA targets a pocket in PYL dimer interface and may stabilize PYL dimer by forming hydrogen networks. Our results illustrate the potential of PYL dimer stabilization in preventing ABA-induced seed germination inhibition. PubMed: 39277642DOI: 10.1038/s41467-024-52426-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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