+Search query
-Structure paper
Title | Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS. |
---|---|
Journal, issue, pages | Protein Sci, Vol. 24, Issue 6, Page 987-995, Year 2015 |
Publish date | Apr 2, 2015 |
Authors | Manuel Fischer / Daniel Rhinow / Zhiwei Zhu / Deryck J Mills / Zongbao K Zhao / Janet Vonck / Martin Grininger / |
PubMed Abstract | Fungal fatty acid synthases Type I (FAS I) are up to 2.7 MDa large molecular machines composed of large multifunctional polypeptides. Half of the amino acids in fungal FAS I are involved in ...Fungal fatty acid synthases Type I (FAS I) are up to 2.7 MDa large molecular machines composed of large multifunctional polypeptides. Half of the amino acids in fungal FAS I are involved in structural elements that are responsible for scaffolding the elaborate barrel-shaped architecture and turning fungal FAS I into highly efficient de novo producers of fatty acids. Rhodosporidium toruloides is an oleaginous fungal species and renowned for its robust conversion of carbohydrates into lipids to over 70% of its dry cell weight. Here, we use cryo-EM to determine a 7.8-Å reconstruction of its FAS I that reveals unexpected features; its novel form of splitting the multifunctional polypeptide chain into the two subunits α and β, and its duplicated ACP domains. We show that the specific distribution into α and β occurs by splitting at one of many possible sites that can be accepted by fungal FAS I. While, therefore, the specific distribution in α and β chains in R. toruloides FAS I is not correlated to increased protein activities, we also show that the duplication of ACP is an evolutionary late event and argue that duplication is beneficial for the lipid overproduction phenotype. |
External links | Protein Sci / PubMed:25761671 / PubMed Central |
Methods | EM (single particle) |
Resolution | 7.8 Å |
Structure data | EMDB-6288: |
Source |
|