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Science 336 (6089): 1708-1711

Copyright © 2012 by the American Association for the Advancement of Science

Structural Basis for Prereceptor Modulation of Plant Hormones by GH3 Proteins

Corey S. Westfall,1,* Chloe Zubieta,2,* Jonathan Herrmann,1 Ulrike Kapp,2 Max H. Nanao,3,4 Joseph M. Jez1,{dagger}

Abstract: Acyl acid amido synthetases of the GH3 family act as critical prereceptor modulators of plant hormone action; however, the molecular basis for their hormone selectivity is unclear. Here, we report the crystal structures of benzoate-specific Arabidopsis thaliana AtGH3.12/PBS3 and jasmonic acid–specific AtGH3.11/JAR1. These structures, combined with biochemical analysis, define features for the conjugation of amino acids to diverse acyl acid substrates and highlight the importance of conformational changes in the carboxyl-terminal domain for catalysis. We also identify residues forming the acyl acid binding site across the GH3 family and residues critical for amino acid recognition. Our results demonstrate how a highly adaptable three-dimensional scaffold is used for the evolution of promiscuous activity across an enzyme family for modulation of plant signaling molecules.

1 Department of Biology, Washington University, St. Louis, MO 63130, USA.
2 European Synchrotron Radiation Facility, 38000 Grenoble, France.
3 European Molecular Biology Laboratory, Grenoble, France.
4 Unit of Virus Host-Cell Interactions, Université Joseph Fourier–European Molecular Biology Laboratory–CNRS, Grenoble, France.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: jjez{at}biology2.wustl.edu


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