Quaternary structure of human fatty acid synthase by electron cryomicroscopy.
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.
Brink
Jacob
J
Verna and Marrs McLean Department of Biochemistry and Molecular Biology and National Center for Macromolecular Imaging, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Ludtke
Steven J
SJ
Yang
Chao-Yuh
CY
Gu
Zei-Wei
ZW
Wakil
Salih J
SJ
Chiu
Wah
W
D001665:Binding Sites; D020285:Cryoelectron Microscopy; D004591:Electrophoresis, Polyacrylamide Gel; D064429:Fatty Acid Synthases / Q000737:chemistry*; D006801:Humans; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D014407:Tumor Cells, Cultured; D014965:X-Rays
D064429:Fatty Acid Synthases