A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors
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Type
ArticleAuthors
Melcher, KarstenNg, Ley-Moy
Zhou, X. Edward
Soon, Fen-Fen
Xu, Yong
Suino-Powell, Kelly M.
Park, Sang-Youl
Weiner, Joshua J.
Fujii, Hiroaki

Chinnusamy, Viswanathan
Kovach, Amanda
Li, Jun
Wang, Yonghong
Li, Jiayang
Peterson, Francis C.
Jensen, Davin R.
Yong, Eu-Leong
Volkman, Brian F.
Cutler, Sean R.
Zhu, Jian-Kang

Xu, H. Eric
KAUST Department
Biological and Environmental Science and Engineering (BESE) DivisionCenter for Desert Agriculture
Plant Stress Genomics Research Lab
Date
2009-12-03Online Publication Date
2009-12-03Print Publication Date
2009-12Permanent link to this record
http://hdl.handle.net/10754/325280
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Show full item recordAbstract
Abscisic acid (ABA) is a ubiquitous hormone that regulates plant growth, development and responses to environmental stresses. Its action is mediated by the PYR/PYL/RCAR family of START proteins, but it remains unclear how these receptors bind ABA and, in turn, how hormone binding leads to inhibition of the downstream type 2C protein phosphatase (PP2C) effectors. Here we report crystal structures of apo and ABA-bound receptors as well as a ternary PYL2-ABA-PP2C complex. The apo receptors contain an open ligand-binding pocket flanked by a gate that closes in response to ABA by way of conformational changes in two highly conserved ?-loops that serve as a gate and latch. Moreover, ABA-induced closure of the gate creates a surface that enables the receptor to dock into and competitively inhibit the PP2C active site. A conserved tryptophan in the PP2C inserts directly between the gate and latch, which functions to further lock the receptor in a closed conformation. Together, our results identify a conserved gate-latch-lock mechanism underlying ABA signalling. © 2009 Macmillan Publishers Limited. All rights reserved.Citation
Melcher K, Ng L-M, Zhou XE, Soon F-F, Xu Y, et al. (2009) A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature 462: 602-608. doi:10.1038/nature08613.Publisher
Springer NatureJournal
NaturePubMed ID
19898420PubMed Central ID
PMC2810868ae974a485f413a2113503eed53cd6c53
10.1038/nature08613
Scopus Count
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