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Title: A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors

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.

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006060
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature (London); Journal Volume: 462; Journal Issue: 12, 2009
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ABSCISIC ACID; CLOSURES; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; HORMONES; PHOSPHATASES; PLANT GROWTH; PROTEINS; STRESSES; TRYPTOPHAN

Citation Formats

Melcher, Karsten, Ng, 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, NU Sinapore), Van Andel), MCW), UCR), and Chinese Aca. Sci.). A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. United States: N. p., 2010. Web. doi:10.1038/nature08613.
Melcher, Karsten, Ng, 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, NU Sinapore), Van Andel), MCW), UCR), & Chinese Aca. Sci.). A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. United States. doi:10.1038/nature08613.
Melcher, Karsten, Ng, 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, NU Sinapore), Van Andel), MCW), UCR), and Chinese Aca. Sci.). Tue . "A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors". United States. doi:10.1038/nature08613.
@article{osti_1006060,
title = {A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors},
author = {Melcher, Karsten and Ng, Ley-Moy and Zhou, X Edward and Soon, Fen-Fen and Xu, Yong and Suino-Powell, Kelly M and Park, Sang-Youl and Weiner, Joshua J and Fujii, Hiroaki and Chinnusamy, Viswanathan and Kovach, Amanda and Li, Jun and Wang, Yonghong and Li, Jiayang and Peterson, Francis C and Jensen, Davin R and Yong, Eu-Leong and Volkman, Brian F and Cutler, Sean R and Zhu, Jian-Kang and Xu, H Eric and NU Sinapore) and Van Andel) and MCW) and UCR) and Chinese Aca. Sci.)},
abstractNote = {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.},
doi = {10.1038/nature08613},
journal = {Nature (London)},
number = 12, 2009,
volume = 462,
place = {United States},
year = {Tue Jan 12 00:00:00 EST 2010},
month = {Tue Jan 12 00:00:00 EST 2010}
}