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

Handle URI:
http://hdl.handle.net/10754/325280
Title:
A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors
Authors:
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 ( 0000-0002-0013-5891 ) ; 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 ( 0000-0001-5134-731X ) ; Xu, H. Eric
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 ?-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.
KAUST Department:
Plant Stress Genomics Research Lab
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 Nature
Journal:
Nature
Issue Date:
3-Dec-2009
DOI:
10.1038/nature08613
PubMed ID:
19898420
PubMed Central ID:
PMC2810868
Type:
Article
ISSN:
00280836
Appears in Collections:
Articles

Full metadata record

DC FieldValue Language
dc.contributor.authorMelcher, Karstenen
dc.contributor.authorNg, Ley-Moyen
dc.contributor.authorZhou, X. Edwarden
dc.contributor.authorSoon, Fen-Fenen
dc.contributor.authorXu, Yongen
dc.contributor.authorSuino-Powell, Kelly M.en
dc.contributor.authorPark, Sang-Youlen
dc.contributor.authorWeiner, Joshua J.en
dc.contributor.authorFujii, Hiroakien
dc.contributor.authorChinnusamy, Viswanathanen
dc.contributor.authorKovach, Amandaen
dc.contributor.authorLi, Junen
dc.contributor.authorWang, Yonghongen
dc.contributor.authorLi, Jiayangen
dc.contributor.authorPeterson, Francis C.en
dc.contributor.authorJensen, Davin R.en
dc.contributor.authorYong, Eu-Leongen
dc.contributor.authorVolkman, Brian F.en
dc.contributor.authorCutler, Sean R.en
dc.contributor.authorZhu, Jian-Kangen
dc.contributor.authorXu, H. Ericen
dc.date.accessioned2014-08-27T09:44:40Zen
dc.date.available2014-08-27T09:44:40Zen
dc.date.issued2009-12-3en
dc.identifier.citationMelcher 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.en
dc.identifier.issn00280836en
dc.identifier.pmid19898420en
dc.identifier.doi10.1038/nature08613en
dc.identifier.urihttp://hdl.handle.net/10754/325280en
dc.description.abstractAbscisic 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.en
dc.language.isoenen
dc.publisherSpringer Natureen
dc.rightsUsers may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#termsen
dc.rightsArchived with thanks to Natureen
dc.subjectabscisic aciden
dc.subjecthormoneen
dc.subjectphosphoprotein phosphatase 2en
dc.subjectabscisic aciden
dc.subjectbiological developmenten
dc.subjectenzyme activityen
dc.subjectgrowth rateen
dc.subjecthormoneen
dc.subjectplant communityen
dc.subjectproteinen
dc.subjectsignalingen
dc.subjectchromatographyen
dc.subjectconformational transitionen
dc.subjectcrystal structureen
dc.subjectenvironmental stressen
dc.subjectgel permeation chromatographyen
dc.subjecthormone bindingen
dc.subjecthormone inhibitionen
dc.subjectligand bindingen
dc.subjectplant developmenten
dc.subjectplant growthen
dc.subjectplant responseen
dc.subjectprotein protein interactionen
dc.subjectAbscisic Aciden
dc.subjectArabidopsisen
dc.subjectArabidopsis Proteinsen
dc.subjectBinding Sitesen
dc.subjectDNA Mutational Analysisen
dc.subjectModels, Molecularen
dc.subjectPlants, Genetically Modifieden
dc.subjectProtein Bindingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectSignal Transductionen
dc.subjectRumexen
dc.titleA gate-latch-lock mechanism for hormone signalling by abscisic acid receptorsen
dc.typeArticleen
dc.contributor.departmentPlant Stress Genomics Research Laben
dc.identifier.journalNatureen
dc.identifier.pmcidPMC2810868en
dc.eprint.versionPost-printen
dc.contributor.institutionLaboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, MI 49503, United Statesen
dc.contributor.institutionDepartment of Obstetrics and Gynecology, National University Hospital, Graduate School for Integrative Sciences and Engineering, Singapore 119074, Singaporeen
dc.contributor.institutionDepartment of Botany and Plant Sciences, University of California at Riverside, Riverside, CA 92521, United Statesen
dc.contributor.institutionDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, United Statesen
dc.contributor.institutionState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, Chinaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorFujii, Hiroakien
kaust.authorChinnusamy, Viswanathanen
kaust.authorZhu, Jian-Kangen

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.