Structural insight into Pichia pastoris fatty acid synthase

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, a...

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Autores principales:	Joseph S. Snowden, Jehad Alzahrani, Lee Sherry, Martin Stacey, David J. Rowlands, Neil A. Ranson, Nicola J. Stonehouse
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ea134c6e98c5470c870f579a6a29ef67
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spelling	oai:doaj.org-article:ea134c6e98c5470c870f579a6a29ef672021-12-02T15:38:12ZStructural insight into Pichia pastoris fatty acid synthase10.1038/s41598-021-89196-22045-2322https://doaj.org/article/ea134c6e98c5470c870f579a6a29ef672021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-89196-2https://doaj.org/toc/2045-2322Abstract 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.Joseph S. SnowdenJehad AlzahraniLee SherryMartin StaceyDavid J. RowlandsNeil A. RansonNicola J. StonehouseNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Joseph S. Snowden Jehad Alzahrani Lee Sherry Martin Stacey David J. Rowlands Neil A. Ranson Nicola J. Stonehouse Structural insight into Pichia pastoris fatty acid synthase
description	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.
format	article
author	Joseph S. Snowden Jehad Alzahrani Lee Sherry Martin Stacey David J. Rowlands Neil A. Ranson Nicola J. Stonehouse
author_facet	Joseph S. Snowden Jehad Alzahrani Lee Sherry Martin Stacey David J. Rowlands Neil A. Ranson Nicola J. Stonehouse
author_sort	Joseph S. Snowden
title	Structural insight into Pichia pastoris fatty acid synthase
title_short	Structural insight into Pichia pastoris fatty acid synthase
title_full	Structural insight into Pichia pastoris fatty acid synthase
title_fullStr	Structural insight into Pichia pastoris fatty acid synthase
title_full_unstemmed	Structural insight into Pichia pastoris fatty acid synthase
title_sort	structural insight into pichia pastoris fatty acid synthase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ea134c6e98c5470c870f579a6a29ef67
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Structural insight into Pichia pastoris fatty acid synthase

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