2WAT

Structure of the fungal type I FAS PPT domain in complex with CoA

2WAT の概要

• エントリーDOI: 10.2210/pdb2wat/pdb
• 関連するPDBエントリー: 2UV8 2VKZ 2WAS
• 分子名称: 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, CHLORIDE ION, COENZYME A, ... (5 entities in total)
• 機能のキーワード: coa, fas, ppt, nad, nadp, transferase, phosphoprotein, oxidoreductase, lipid synthesis, phosphopantetheine transferase, phosphopantetheine, multifunctional enzyme, fatty acid biosynthesis, phosphopantetheinylation
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 80806.60

構造登録者

Johansson, P.,Mulincacci, B.,Koestler, C.,Grininger, M. (登録日: 2009-02-15, 公開日: 2009-08-25, 最終更新日: 2024-05-08)

主引用文献

Johansson, P.,Mulinacci, B.,Koestler, C.,Vollrath, R.,Oesterhelt, D.,Grininger, M.
Multimeric Options for the Auto-Activation of the Saccharomyces Cerevisiae Fas Type I Megasynthase.
Structure, 17:1063-, 2009

PubMed Abstract: The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT). However, recent X-ray structures of the fungal FAS revealed a barrel-shaped architecture, with PPT located at the outside of the barrel wall, spatially separated from the ACP caged in the inner volume. This separation indicated that the activation has to proceed before the assembly to the mature complex, in a conformation where the ACP and PPT domains can meet. To gain insight into the auto-activation reaction and also into the fungal FAS assembly pathway, we structurally and functionally characterized the Saccharomyces cerevisiae FAS type I PPT as part of the multienzyme protein and as an isolated domain.

PubMed: 19679086
DOI: 10.1016/J.STR.2009.06.014

実験手法

X-RAY DIFFRACTION (2.2 Å)