8A6Z

PcIDS1 in complex with Mn2+ and IPP

8A6Z の概要

• エントリーDOI: 10.2210/pdb8a6z/pdb
• 関連するPDBエントリー: 8A6U
• 分子名称: Isoprenyl diphosphate synthase, MANGANESE (II) ION, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: insects, biosynthesis, terpenes, metal regulation, catalysis, biosynthetic protein
• 由来する生物種: Phaedon cochleariae (mustard beetle)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 244150.14

構造登録者

Ecker, F.,Boland, W.,Groll, M. (登録日: 2022-06-20, 公開日: 2023-05-31, 最終更新日: 2024-02-07)

主引用文献

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

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: 37308711
DOI: 10.1038/s41557-023-01235-9

実験手法

X-RAY DIFFRACTION (2.4 Å)