9FXD
Structure of indole-3-acetic acid-amido synthetase GH3.6 from A.thaliana in complex with AMP and aspartate
Summary for 9FXD
| Entry DOI | 10.2210/pdb9fxd/pdb |
| Related | 9FWD |
| Descriptor | Indole-3-acetic acid-amido synthetase GH3.6, ADENOSINE MONOPHOSPHATE, ASPARTIC ACID, ... (4 entities in total) |
| Functional Keywords | enzyme complex, amp, aspartate, ligase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 140963.55 |
| Authors | Kopecny, D.,Briozzo, P. (deposition date: 2024-07-01, release date: 2025-04-09, Last modification date: 2025-09-03) |
| Primary citation | Hladik, P.,Brunoni, F.,Zukauskaite, A.,Zatloukal, M.,Belicek, J.,Kopecny, D.,Briozzo, P.,Ferchaud, N.,Novak, O.,Pencik, A. Phenylacetic acid metabolism in land plants: novel pathways and metabolites. J.Exp.Bot., 76:3427-3443, 2025 Cited by PubMed Abstract: In recent years, substantial progress has been made in exploring auxin conjugation and metabolism, primarily aiming at indole-3-acetic acid (IAA). However, the metabolic regulation of another key auxin, phenylacetic acid (PAA), remains largely uncharacterized. Here, we provide a comprehensive exploration of PAA metabolism in land plants. Through LC-MS screening across multiple plant species and their organs, we identified four previously unreported endogenous PAA metabolites: phenylacetyl-leucine (PAA-Leu), phenylacetyl-phenylalanine (PAA-Phe), phenylacetyl-valine (PAA-Val), and phenylacetyl-glucose (PAA-glc). Enzyme assays, genetic evidence, crystal structures, and docking studies demonstrate that PAA and IAA share core metabolic machinery, revealing a complex regulatory network that maintains auxin homeostasis. Furthermore, our study of PAA conjugation with amino acids and glucose suggests limited compensatory mechanisms within known conjugation pathways, pointing to the existence of alternative metabolic routes in land plants. These insights advance our knowledge of auxin-specific metabolic networks and highlight the unique complexity within plant hormone regulation. PubMed: 40130494DOI: 10.1093/jxb/eraf092 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.736 Å) |
Structure validation
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