TY - JOUR
T1 - Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a unique regulatory mechanism
AU - Zhang, Xingliang
AU - Zhang, Qi
AU - Xin, Qi
AU - Yu, Lin
AU - Wang, Zheng
AU - Wu, Wei
AU - Jiang, Lun
AU - Wang, Guoqiang
AU - Tian, Wenli
AU - Deng, Zengqin
AU - Wang, Yang
AU - Liu, Zhao
AU - Long, Jiafu
AU - Gong, Zhizhong
AU - Chen, Zhongzhou
N1 - Funding Information:
We thank Dr. Dawei Li for generously providing us experiment condition during the early stage of this project. We thank Dr. De Ye for discussion. The synchrotron-radiation experiments were performed at SSRF beamline BL17U, BSRF beamline 1W2B, NE3A (KEK) and Spring-8 beamline BL41XU. This work was supported by National Basic Research Program of China (973 Program, 2011CB965304 and 2009CB825501), National Natural Science Foundation of China (31070664 and 90919043), Transgenic project (2009ZX08010-004B), Fok Ying Tung Education Foundation (121025), and National Laboratory of Medical Molecular Biology. Z.D. was supported by National Natural Science Foundation of China (J0730639).
PY - 2012/5/9
Y1 - 2012/5/9
N2 - 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 unexpected trans-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 the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.
AB - 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 unexpected trans-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 the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.
UR - https://www.scopus.com/pages/publications/84861021136
U2 - 10.1016/j.str.2012.02.019
DO - 10.1016/j.str.2012.02.019
M3 - Article
C2 - 22579247
AN - SCOPUS:84861021136
SN - 0969-2126
VL - 20
SP - 780
EP - 790
JO - Structure
JF - Structure
IS - 5
ER -