Fig. 4: DBSA targets PYL1 dimer interface and stabilizes the PYL1 dimer via hydrogen bond networks. | Nature Communications

Fig. 4: DBSA targets PYL1 dimer interface and stabilizes the PYL1 dimer via hydrogen bond networks.

From: Stabilization of dimeric PYR/PYL/RCAR family members relieves abscisic acid-induced inhibition of seed germination

Fig. 4

a Crystal structure of PYL1 with DBSA (PDB code 9J6I, green) and ABA (PDB code 3JRS, yellow). ABA induced a gate-close and latch-close conformation, which DBSA bind to a DBSA induced a gate-open and latch- open conformation. b PYL1 was maintained in the latch-open and gate-open state in the crystal structure (shown in green stick model). DBSA forms hydrogen bonds with the side chain of Arg143. DBSA was predicted to bind to latch-open and gate-open PYR1 and interact with R116 (shown in pink stick model). c Alanine mutation result showed that DBSA may form strong interaction with R116 of PYR1. d The aggregation states of PYR1 dimer induced by ABA, DBSA or ABA/DBSA co-treatment were detected by SEC-MALLS. e The motion trends of ABA-PYR1 and DBSA-PYL1 complexes. f The dominant conformations were determined using FEL analysis. g The hydrogen networks mediated by ABA of PYR1 or DBSA of PYL1 in the dimer interfaces.

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