Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism.
Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism.
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DOI:
10.1016/j.str.2012.02.019
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发表时间:
2012-05
期刊:
影响因子:
5.7
通讯作者:
Xingliang Zhang;Qi Zhang;Qi Xin;Lin Yu;Z. Wang;Wei Wu;Lun Jiang;Guoqiang Wang;Wenli Tian-Wenli-Tia
中科院分区:
文献类型:
--
作者:
Xingliang Zhang;Qi Zhang;Qi Xin;Lin Yu;Z. Wang;Wei Wu;Lun Jiang;Guoqiang Wang;Wenli Tian-Wenli-Tia
Abscisic acid (ABA) controls many physiological processes and mediates adaptive responses to abiotic stresses. The ABA signaling mechanisms for abscisic acid receptors PYR/PYL/RCAR (PYLs) were reported. However, it remains unclear whether the molecular mechanisms are suitable for other PYLs. Here, complex structures of PYL3 with (+)-ABA, pyrabactin and HAB1 are reported. An unexpectedtrans-homodimer intermediate observed in the crystal is confirmed in solution. ABA-bound PYL3 greatly promotes the generation of monomeric PYL3, which can excessively increase the efficiency of inhibiting PP2Cs. Structure-guided biochemical experiments show that Ser195 accounts for the key intermediate. Interestingly, pyrabactin binds to PYL3 in a distinct nonproductive mode with gate closure, which sheds light on the design of agonists and antagonists for abscisic acid receptors. According to different conformations of ligand-bound PYLs, the PYLs family can be divided into three subclasses, among which thetrans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.