6SM6

AntF (holo): type II PKS acyl-carrier protein

6SM6 の概要

• エントリーDOI: 10.2210/pdb6sm6/pdb
• 関連するPDBエントリー: 6SM4
• 分子名称: Acyl carrier protein (2 entities in total)
• 機能のキーワード: natural product biosynthesis, polyketides, minimal pks system, anthraquinone, chain elongation, catalysis, protein binding
• 由来する生物種: Photorhabdus luminescens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22382.42

構造登録者

Braeuer, A.,Zhou, Q.,Grammbitter, G.L.C.,Schmalhofer, M.,Ruehl, M.,Kaila, V.R.I.,Bode, H.,Groll, M. (登録日: 2019-08-21, 公開日: 2020-05-27, 最終更新日: 2024-01-24)

主引用文献

Brauer, A.,Zhou, Q.,Grammbitter, G.L.C.,Schmalhofer, M.,Ruhl, M.,Kaila, V.R.I.,Bode, H.B.,Groll, M.
Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis.
Nat.Chem., 12:755-763, 2020

PubMed Abstract: Type II polyketide synthases (PKSs) are multi-enzyme complexes that produce secondary metabolites of medical relevance. Chemical backbones of such polyketides are produced by minimal PKS systems that consist of a malonyl transacylase, an acyl carrier protein and an α/β heterodimeric ketosynthase. Here, we present X-ray structures of all ternary complexes that constitute the minimal PKS system for anthraquinone biosynthesis in Photorhabdus luminescens. In addition, we characterize this invariable core using molecular simulations, mutagenesis experiments and functional assays. We show that malonylation of the acyl carrier protein is accompanied by major structural rearrangements in the transacylase. Principles of an ongoing chain elongation are derived from the ternary complex with a hexaketide covalently linking the heterodimeric ketosynthase with the acyl carrier protein. Our results for the minimal PKS system provide mechanistic understanding of PKSs and a fundamental basis for engineering PKS pathways for future applications.

PubMed: 32632186
DOI: 10.1038/s41557-020-0491-7

実験手法

X-RAY DIFFRACTION (2.4 Å)