4EPM
Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP
Summary for 4EPM
| Entry DOI | 10.2210/pdb4epm/pdb |
| Related | 4EPL 4EQL 4EWV |
| Descriptor | 4-substituted benzoates-glutamate ligase GH3.12, ADENOSINE MONOPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | anl superfamily, acyl acid-amido synthetase, adenylation, ligase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 66205.71 |
| 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 Cited by 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: 22628555DOI: 10.1126/science.1221863 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.099 Å) |
Structure validation
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