7BC4

Cryo-EM structure of fatty acid synthase (FAS) from Pichia pastoris

7BC4 の概要

• エントリーDOI: 10.2210/pdb7bc4/pdb
• EMDBエントリー: 12138
• 分子名称: Fatty acid synthase subunit alpha, Fatty acid synthase subunit beta, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: multienzyme, complex, fatty acid, synthase, biosynthetic protein
• 由来する生物種: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 436832.70

構造登録者

Snowden, J.S.,Alzahrani, J.,Sherry, L.,Stacey, M.,Rowlands, D.J.,Ranson, N.A.,Stonehouse, N.J. (登録日: 2020-12-18, 公開日: 2021-05-19, 最終更新日: 2025-10-01)

主引用文献

Snowden, J.S.,Alzahrani, J.,Sherry, L.,Stacey, M.,Rowlands, D.J.,Ranson, N.A.,Stonehouse, N.J.
Structural insight into Pichia pastoris fatty acid synthase.
Sci Rep, 11:9773-9773, 2021

PubMed Abstract: Type I fatty acid synthases (FASs) are critical metabolic enzymes which are common targets for bioengineering in the production of biofuels and other products. Serendipitously, we identified FAS as a contaminant in a cryoEM dataset of virus-like particles (VLPs) purified from P. pastoris, an important model organism and common expression system used in protein production. From these data, we determined the structure of P. pastoris FAS to 3.1 Å resolution. While the overall organisation of the complex was typical of type I FASs, we identified several differences in both structural and enzymatic domains through comparison with the prototypical yeast FAS from S. cerevisiae. Using focussed classification, we were also able to resolve and model the mobile acyl-carrier protein (ACP) domain, which is key for function. Ultimately, the structure reported here will be a useful resource for further efforts to engineer yeast FAS for synthesis of alternate products.

PubMed: 33963233
DOI: 10.1038/s41598-021-89196-2

実験手法

ELECTRON MICROSCOPY (3.1 Å)