4EPL

Crystal Structure of Arabidopsis thaliana GH3.11 (JAR1) in Complex with JA-Ile

Summary for 4EPL

• Entry DOI: 10.2210/pdb4epl/pdb
• Related: 4EPM 4EQL 4EWV
• Descriptor: Jasmonic acid-amido synthetase JAR1, N-({(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetyl)-L-isoleucine (3 entities in total)
• Functional Keywords: anl adenylating enzyme, acyl acid-amido synthetase, adenylation, ligase
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cytoplasm: Q9SKE2
• Total number of polymer chains: 1
• Total formula weight: 65381.36

Authors

Westfall, C.S.,Zubieta, C.,Herrmann, J.,Kapp, U.,Nanao, M.H.,Jez, J.M. (deposition date: 2012-04-17, release date: 2012-06-20, Last modification date: 2024-02-28)

Primary citation

Westfall, C.S.,Zubieta, C.,Herrmann, J.,Kapp, U.,Nanao, M.H.,Jez, J.M.
Structural basis for prereceptor modulation of plant hormones by GH3 proteins.
Science, 336:1708-1711, 2012

PubMed 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.

PubMed: 22628555
DOI: 10.1126/science.1221863

Experimental method

X-RAY DIFFRACTION (2.007 Å)