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 beta-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.

journal_name

Nature

journal_title

Nature

authors

Melcher K,Ng LM,Zhou XE,Soon FF,Xu Y,Suino-Powell KM,Park SY,Weiner JJ,Fujii H,Chinnusamy V,Kovach A,Li J,Wang Y,Li J,Peterson FC,Jensen DR,Yong EL,Volkman BF,Cutler SR,Zhu JK,Xu HE

doi

10.1038/nature08613

subject

Has Abstract

pub_date

2009-12-03 00:00:00

pages

602-8

issue

7273

eissn

0028-0836

issn

1476-4687

pii

nature08613

journal_volume

462

pub_type

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