Quaternary structure of human fatty acid synthase by electron cryomicroscopy

Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):138-43. doi: 10.1073/pnas.012589499. Epub 2001 Dec 26.


We present the first three-dimensional reconstruction of human fatty acid synthase obtained by electron cryomicroscopy and single-particle image processing. The structure shows that the synthase is composed of two monomers, arranged in an antiparallel orientation, which is consistent with biochemical data. The monomers are connected to each other at their middle by a bridge of density, a site proposed to be the combination of the interdomain regions of the two monomers. Each monomer subunit appears to be subdivided into three structural domains. With this reconstruction of the synthase, we propose a location for the enzyme's two fatty acid synthesis sites.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Cryoelectron Microscopy
  • Electrophoresis, Polyacrylamide Gel
  • Fatty Acid Synthases / chemistry*
  • Humans
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Scattering, Radiation
  • Tumor Cells, Cultured
  • X-Rays


  • Fatty Acid Synthases