8A7K
PcIDS1 in complex with Mg2+/Mn2+, IPP, and ZOL
Summary for 8A7K
| Entry DOI | 10.2210/pdb8a7k/pdb |
| Related | 8A6U |
| Descriptor | Isoprenyl diphosphate synthase, MANGANESE (II) ION, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | insects, biosynthesis, terpenes, metal regulation, catalysis, biosynthetic protein |
| Biological source | Phaedon cochleariae (mustard beetle) |
| Total number of polymer chains | 2 |
| Total formula weight | 81746.03 |
| Authors | Ecker, F.,Boland, W.,Groll, M. (deposition date: 2022-06-21, release date: 2023-05-31, Last modification date: 2024-02-07) |
| Primary citation | Ecker, F.,Vattekkatte, A.,Boland, W.,Groll, M. Metal-dependent enzyme symmetry guides the biosynthetic flux of terpene precursors. Nat.Chem., 15:1188-1195, 2023 Cited by PubMed Abstract: Terpenoids account for more than 60% of all natural products, and their carbon skeletons originate from common isoprenoid units of different lengths such as geranyl pyrophosphate and farnesyl pyrophosphate. Here we characterize a metal-dependent, bifunctional isoprenyl diphosphate synthase from the leaf beetle Phaedon cochleariae by structural and functional analyses. Inter- and intramolecular cooperative effects in the homodimer strongly depend on the provided metal ions and regulate the biosynthetic flux of terpene precursors to either biological defence or physiological development. Strikingly, a unique chain length determination domain adapts to form geranyl or farnesyl pyrophosphate by altering enzyme symmetry and ligand affinity between both subunits. In addition, we identify an allosteric geranyl-pyrophosphate-specific binding site that shares similarity with end-product inhibition in human farnesyl pyrophosphate synthase. Our combined findings elucidate a deeply intertwined reaction mechanism in the P. cochleariae isoprenyl diphosphate synthase that integrates substrate, product and metal-ion concentrations to harness its dynamic potential. PubMed: 37308711DOI: 10.1038/s41557-023-01235-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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