A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors

Karsten Melcher, Ley-Moy Ng, X. Edward Zhou, Fen-Fen Soon, Yong Xu, Kelly M. Suino-Powell, Sang-Youl Park, Joshua J. Weiner, Hiroaki Fujii, Viswanathan Chinnusamy, Amanda Kovach, Jun Li, Yonghong Wang, Jiayang Li, Francis C. Peterson, Davin R. Jensen, Eu-Leong Yong, Brian F. Volkman, Sean R. Cutler, Jian-Kang Zhu and H. Eric Xu ()
Additional contact information
Karsten Melcher: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Ley-Moy Ng: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
X. Edward Zhou: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Fen-Fen Soon: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Yong Xu: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Kelly M. Suino-Powell: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Sang-Youl Park: University of California at Riverside, Riverside, California 92521, USA
Joshua J. Weiner: Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA
Hiroaki Fujii: University of California at Riverside, Riverside, California 92521, USA
Viswanathan Chinnusamy: University of California at Riverside, Riverside, California 92521, USA
Amanda Kovach: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Jun Li: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
Yonghong Wang: State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, National Center for Plant Gene Research
Jiayang Li: State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, National Center for Plant Gene Research
Francis C. Peterson: Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA
Davin R. Jensen: Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA
Eu-Leong Yong: National University Hospital, Yong Loo Lin School of Medicine, Graduate School for Integrative Sciences & Engineering, National University of Singapore
Brian F. Volkman: Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA
Sean R. Cutler: University of California at Riverside, Riverside, California 92521, USA
Jian-Kang Zhu: University of California at Riverside, Riverside, California 92521, USA
H. Eric Xu: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA

Nature, 2009, vol. 462, issue 7273, 602-608

Abstract: Abstract 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 β-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.

Date: 2009
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DOI: 10.1038/nature08613

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