+検索条件
-Structure paper
タイトル | Structural insight into Pichia pastoris fatty acid synthase. |
---|---|
ジャーナル・号・ページ | Sci Rep, Vol. 11, Issue 1, Page 9773, Year 2021 |
掲載日 | 2021年5月7日 |
著者 | Joseph S Snowden / Jehad Alzahrani / Lee Sherry / Martin Stacey / David J Rowlands / Neil A Ranson / Nicola J Stonehouse / |
PubMed 要旨 | 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 ...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. |
リンク | Sci Rep / PubMed:33963233 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 Å |
構造データ | EMDB-12138, PDB-7bc4: EMDB-12139: Fatty acid synthase (FAS) from Pichia pastoris, including ACP domain resolved by focussed classification |
化合物 | ChemComp-FMN: |
由来 |
|
キーワード | BIOSYNTHETIC PROTEIN / Multienzyme / Complex / Fatty acid / Synthase |