The abscisic acid receptor PYR1 in complex with abscisic acid.

Détails

ID Serval
serval:BIB_B6A142D2C262
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The abscisic acid receptor PYR1 in complex with abscisic acid.
Périodique
Nature
Auteur(s)
Santiago J., Dupeux F., Round A., Antoni R., Park S.Y., Jamin M., Cutler S.R., Rodriguez P.L., Márquez J.A.
ISSN
1476-4687 (Electronic)
ISSN-L
0028-0836
Statut éditorial
Publié
Date de publication
03/12/2009
Peer-reviewed
Oui
Volume
462
Numéro
7273
Pages
665-668
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
The plant hormone abscisic acid (ABA) has a central role in coordinating the adaptive response in situations of decreased water availability as well as the regulation of plant growth and development. Recently, a 14-member family of intracellular ABA receptors, named PYR/PYL/RCAR, has been identified. These proteins inhibit in an ABA-dependent manner the activity of a family of key negative regulators of the ABA signalling pathway: the group-A protein phosphatases type 2C (PP2Cs). Here we present the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. In the ligand-bound subunit, the loops surrounding the entry to the binding cavity fold over the ABA molecule, enclosing it inside, whereas in the empty subunit they form a channel leaving an open access to the cavity, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone-receptor complex. By providing structural details on the ABA-binding pocket, this work paves the way for the development of new small molecules able to activate the plant stress response.
Mots-clé
Abscisic Acid/metabolism, Arabidopsis, Arabidopsis Proteins/chemistry, Arabidopsis Proteins/metabolism, Membrane Transport Proteins/chemistry, Membrane Transport Proteins/metabolism, Models, Molecular, Protein Binding, Protein Structure, Tertiary
Pubmed
Web of science
Création de la notice
10/01/2019 18:24
Dernière modification de la notice
21/08/2019 6:35
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