7BC5

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

Summary for 7BC5

• Entry DOI: 10.2210/pdb7bc5/pdb
• EMDB information: 12139
• Descriptor: Fatty acid synthase subunit alpha (1 entity in total)
• Functional Keywords: multienzyme, complex, fatty acid, synthase, biosynthetic protein
• Biological source: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast)
• Total number of polymer chains: 1
• Total formula weight: 206375.73

Authors

Snowden, J.S.,Alzahrani, J.,Sherry, L.,Stacey, M.,Rowlands, D.J.,Ranson, N.A.,Stonehouse, N.J. (deposition date: 2020-12-18, release date: 2021-05-19, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.1 Å)