6FIJ

Structure of the loading/condensing region (SAT-KS-MAT) of the cercosporin fungal non-reducing polyketide synthase (NR-PKS) CTB1

6FIJ の概要

• エントリーDOI: 10.2210/pdb6fij/pdb
• 関連するPDBエントリー: 6FIK
• EMDBエントリー: 4266
• 分子名称: Polyketide synthase, 1,2-ETHANEDIOL, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: nr-pks, pks, ipks, iterative pks, non-reducing, sat, starter acyl, condensing, loading, polyketide, fungal, biosynthetic protein
• 由来する生物種: Cercospora nicotianae (Barn spot disease fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 281713.68

構造登録者

Herbst, D.A.,Jakob, R.P.,Townsend, C.A.,Maier, T. (登録日: 2018-01-18, 公開日: 2018-03-21, 最終更新日: 2024-01-17)

主引用文献

Herbst, D.A.,Huitt-Roehl, C.R.,Jakob, R.P.,Kravetz, J.M.,Storm, P.A.,Alley, J.R.,Townsend, C.A.,Maier, T.
The structural organization of substrate loading in iterative polyketide synthases.
Nat. Chem. Biol., 14:474-479, 2018

PubMed Abstract: Polyketide synthases (PKSs) are microbial multienzymes for the biosynthesis of biologically potent secondary metabolites. Polyketide production is initiated by the loading of a starter unit onto an integral acyl carrier protein (ACP) and its subsequent transfer to the ketosynthase (KS). Initial substrate loading is achieved either by multidomain loading modules or by the integration of designated loading domains, such as starter unit acyltransferases (SAT), whose structural integration into PKS remains unresolved. A crystal structure of the loading/condensing region of the nonreducing PKS CTB1 demonstrates the ordered insertion of a pseudodimeric SAT into the condensing region, which is aided by the SAT-KS linker. Cryo-electron microscopy of the post-loading state trapped by mechanism-based crosslinking of ACP to KS reveals asymmetry across the CTB1 loading/-condensing region, in accord with preferential 1:2 binding stoichiometry. These results are critical for re-engineering the loading step in polyketide biosynthesis and support functional relevance of asymmetric conformations of PKSs.

PubMed: 29610486
DOI: 10.1038/s41589-018-0026-3

実験手法

X-RAY DIFFRACTION (2.77 Å)