Structural Basis for Prereceptor Modulation of Plant Hormones by GH3 Proteins

Journal Article · Mon Apr 08 00:00:00 EDT 2013 · Science

DOI:https://doi.org/10.1126/scisignal.2003353· OSTI ID:1045685

Westfall, Corey S; Zubieta, Chloe; Herrmann, Jonathan; Kapp, Ulrike; Nanao, Max H; Jez, Joseph M ^[1]

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1. WU

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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: NSFOTHERUSDAHHMI
• OSTI ID: 1045685
• Journal Information: Science, Vol. 336, Issue 06, 2012; ISSN 0036-8075
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
AMINO ACIDS
ARABIDOPSIS
CATALYSIS
CONFORMATIONAL CHANGES
CRYSTAL STRUCTURE
ENZYMES
HORMONES
LIGASES
MODULATION
PROTEINS
RESIDUES
SUBSTRATES