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Structural insight into Pichia pastoris fatty acid synthase

Title: Structural insight into Pichia pastoris fatty acid synthase
Authors: Snowden, JS; Alzahrani, J; Sherry, L; Stacey, M; Rowlands, DJ; Ranson, NA; Stonehouse, NJ
Publisher Information: Nature Research
Publication Year: 2021
Collection: White Rose Research Online (Universities of Leeds, Sheffield & York)
Description: 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.
Document Type: article in journal/newspaper
File Description: text
Language: English
ISSN: 2045-2322
Relation: https://eprints.whiterose.ac.uk/id/eprint/173211/6/s41598-021-89196-2.pdf; Snowden, JS orcid.org/0000-0001-7857-0634 , Alzahrani, J, Sherry, L orcid.org/0000-0002-4367-772X et al. (4 more authors) (2021) Structural insight into Pichia pastoris fatty acid synthase. Scientific Reports, 11. 9773. ISSN: 2045-2322
Availability: https://eprints.whiterose.ac.uk/id/eprint/173211/
Rights: cc_by_4
Accession Number: edsbas.E96F34AB
Database: BASE