Letter | Published:

The abscisic acid receptor PYR1 in complex with abscisic acid

Nature volume 462, pages 665668 (03 December 2009) | Download Citation

Abstract

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/RCAR1,2,3, 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)4,5,6. 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.

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Protein Data Bank

Data deposits

Atomic coordinates and structure factors for the reported crystal structure have been deposited in the Protein Data Bank under accession code 3K90.

References

  1. 1.

    et al. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science 324, 1068–1071 (2009)

  2. 2.

    et al. Regulators of PP2C phosphatase activity function as abscisic acid sensors. Science 324, 1064–1068 (2009)

  3. 3.

    et al. Modulation of drought resistance by the abscisic acid-receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 10.1111/j.1365-313X.2009.03981.x (16 July 2009)

  4. 4.

    et al. Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science 264, 1448–1452 (1994)

  5. 5.

    , & A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science 264, 1452–1455 (1994)

  6. 6.

    et al. Triple loss of function of protein phosphatases type 2C leads to partial constitutive response to endogenous abscisic acid. Plant Physiol. 150, 1345–1355 (2009)

  7. 7.

    , , , & Methods and concepts in quantifying resistance to drought, salt and freezing, abiotic stresses that affect plant water status. Plant J. 45, 523–539 (2006)

  8. 8.

    , & Two novel GPCR-type G proteins are abscisic acid receptors in Arabidopsis. Cell 136, 136–148 (2009)

  9. 9.

    & Are GTGs ABA’s biggest fans? Cell 136, 21–23 (2009)

  10. 10.

    , & The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol. Biol. 8, 286 (2008)

  11. 11.

    , & Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily. Proteins 43, 134–144 (2001)

  12. 12.

    et al. Unphosphorylated rhabdoviridae phosphoproteins form elongated dimers in solution. Biochemistry 46, 10328–10338 (2007)

  13. 13.

    & START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem. Sci. 24, 130–132 (1999)

  14. 14.

    & The crystal and molecular structure of dl-2-cis-4-trans-abscisic acid. Bull. Chem. Soc. Jpn 50, 1506–1509 (1997)

  15. 15.

    The chemistry and physiology of abscisic acid. Annu. Rev. Plant Physiol. 25, 259–307 (1974)

  16. 16.

    , , , & HAB1–SWI3B interaction reveals a link between abscisic acid signaling and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis. Plant Cell 20, 2972–2988 (2008)

  17. 17.

    Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795–800 (1993)

  18. 18.

    & Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)

  19. 19.

    , & Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240–255 (1997)

  20. 20.

    et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007)

  21. 21.

    , , , & PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Crystallogr. 36, 1277–1282 (2003)

  22. 22.

    , & CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768–773 (1995)

  23. 23.

    , & LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127–134 (1995)

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Acknowledgements

We thank A. McArthy and S. Brockhauser for support during X-ray data collection and R. Serrano and S. Cusack for critical reading of the manuscript. We are grateful to the European Synchrotron radiation facility (ESRF) and the EMBL for access to the macromolecular crystallography and BioSAXS beamlines. This work was supported by grant BIO2008-00221 from Ministerio de Educación y Ciencia and Fondo Europeo de Desarrollo Regional and Consejo Superior de Investigaciones Científicas (fellowships to J.S. and R.A.). Access to the high throughput crystallization facility of the Partnership for Structural Biology in Grenoble (PSB) (https://htxlab.embl.fr) was supported by the European Community–Research Infrastructure Action PCUBE under the FP7 ‘Capacities’ specific programme.

Author Contributions J.S. contributed with the cloning, protein purification, ITC, MALLS and helped with crystallization and SAXS experiments. F.D. performed protein purification, crystallization and crystal refinement experiments and helped with X-ray data collection. A.R. supervised SAXS data collection and performed data analysis. M.J. carried out MALLS experiments and analysis. R.A. carried out cloning and protein purification. S.-Y.P. and S.R.C. carried out cloning of mutant PYR1 proteins and contributed to discussions. P.L.R. contributed to discussions and writing of the manuscript. J.A.M. supervised the work and performed data collection, structure solution and refinement as well as writing of the manuscript.

Author information

Author notes

    • Julia Santiago
    •  & Florine Dupeux

    These authors contributed equally to this work.

Affiliations

  1. Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, Spain

    • Julia Santiago
    • , Regina Antoni
    •  & Pedro Luis Rodriguez
  2. European Molecular Biology Laboratory, Grenoble Outstation and Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France

    • Florine Dupeux
    • , Adam Round
    •  & José Antonio Márquez
  3. Department of Botany and Plant Sciences. Center for Plant Cell Biology. University of California, Riverside, California 92521, USA

    • Sang-Youl Park
    •  & Sean R. Cutler
  4. Virus Host Cell Interactions (UVHCI) UMI 3265, Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France

    • Marc Jamin

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Competing interests

A patent application is in progress.

Corresponding author

Correspondence to José Antonio Márquez.

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    Supplementary Information

    This file contains Supplementary Tables 1-2, Supplementary Notes and Data, Supplementary References and Supplementary Figures S1-S3 with Legends.

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DOI

https://doi.org/10.1038/nature08591

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