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| Title | Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 107, Issue 20, Page 9164-9169, Year 2010 |
| Publish date | May 18, 2010 |
 Authors | Preeti Gipson / Deryck J Mills / Remco Wouts / Martin Grininger / Janet Vonck / Werner Kühlbrandt /  |
| PubMed Abstract | Yeast fatty acid synthase (FAS) is a 2.6-MDa barrel-shaped multienzyme complex, which carries out cyclic synthesis of fatty acids. By electron cryomicroscopy of single particles we obtained a three- ...Yeast fatty acid synthase (FAS) is a 2.6-MDa barrel-shaped multienzyme complex, which carries out cyclic synthesis of fatty acids. By electron cryomicroscopy of single particles we obtained a three-dimensional map of yeast FAS at 5.9-A resolution. Compared to the crystal structures of fungal FAS, the EM map reveals major differences and new features that indicate a considerably different arrangement of the complex in solution compared to the crystal structures, as well as a high degree of variance inside the barrel. Distinct density regions in the reaction chambers next to each of the catalytic domains fitted the substrate-binding acyl carrier protein (ACP) domain. In each case, this resulted in the expected distance of approximately 18 A from the ACP substrate-binding site to the active site of the catalytic domains. The multiple, partially occupied positions of the ACP within the reaction chamber provide direct structural insight into the substrate-shuttling mechanism of fatty acid synthesis in this large cellular machine. |
 External links | Proc Natl Acad Sci U S A / PubMed:20231485 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 5.9 Å |
| Structure data |  EMDB-1623: |
| Source |
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Saccharomyces cerevisiae (brewer's yeast)