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7ZMD

Ketosynthase domain of module 3 from Brevibacillus Brevis orphan BGC11

7ZMD の概要
エントリーDOI10.2210/pdb7zmd/pdb
EMDBエントリー14795
分子名称Putative polyketide synthase (1 entity in total)
機能のキーワードketosynthase, polyketide synthase, thiolase fold, claisen condensation, 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374849.56
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: 2024-07-24)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.93 Å)
構造検証レポート
Validation report summary of 7zmd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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