Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy.

@article{Gipson2010DirectSI,
  title={Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy.},
  author={Preeti Gipson and Deryck J Mills and Remco Wouts and Martin Grininger and Janet Vonck and Werner K{\"u}hlbrandt},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 20},
  pages={9164-9}
}
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… CONTINUE READING

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