7ZMF

Dehydratase domain of module 3 from Brevibacillus Brevis orphan BGC11

7ZMF の概要

• エントリーDOI: 10.2210/pdb7zmf/pdb
• 分子名称: Putative polyketide synthase, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: dehydratase, polyketide synthase, double hot dog fold, biosynthetic protein
• 由来する生物種: Brevibacillus brevis NBRC 100599
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66996.35

構造登録者

Tittes, Y.U.,Herbst, D.A.,Jakob, R.P.,Maier, T. (登録日: 2022-04-19, 公開日: 2022-09-21, 最終更新日: 2024-02-07)

主引用文献

Tittes, Y.U.,Herbst, D.A.,Martin, S.F.X.,Munoz-Hernandez, H.,Jakob, R.P.,Maier, T.
The structure of a polyketide synthase bimodule core.
Sci Adv, 8:eabo6918-eabo6918, 2022

PubMed Abstract: Polyketide synthases (PKSs) are predominantly microbial biosynthetic enzymes. They assemble highly potent bioactive natural products from simple carboxylic acid precursors. The most versatile families of PKSs are organized as assembly lines of functional modules. Each module performs one round of precursor extension and optional modification, followed by directed transfer of the intermediate to the next module. While enzymatic domains and even modules of PKSs are well understood, the higher-order modular architecture of PKS assembly lines remains elusive. Here, we visualize a PKS bimodule core using cryo-electron microscopy and resolve a two-dimensional meshwork of the bimodule core formed by homotypic interactions between modules. The sheet-like organization provides the framework for efficient substrate transfer and for sequestration of trans-acting enzymes required for polyketide production.

PubMed: 36129979
DOI: 10.1126/sciadv.abo6918

実験手法

X-RAY DIFFRACTION (2.21 Å)