期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 16, 期 2, 页码 190-197出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1532
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资金
- US National Institutes of Health [F32 DK080622, RO1 DK16073]
The metazoan cytosolic fatty acid synthase (FAS) contains all of the enzymes required for de novo fatty acid biosynthesis covalently linked around two reaction chambers. Although the three-dimensional architecture of FAS has been mostly defined, it is unclear how reaction intermediates can transfer between distant catalytic domains. Using single-particle EM, we have identified a near continuum of conformations consistent with a remarkable flexibility of FAS. The distribution of conformations was influenced by the presence of substrates and altered by different catalytic mutations, suggesting a direct correlation between conformation and specific enzymatic activities. We interpreted three-dimensional reconstructions by docking high-resolution structures of individual domains, and they show that the substrate-loading and condensation domains dramatically swing and swivel to access substrates within either reaction chamber. Concomitant rearrangement of the beta-carbon -processing domains synchronizes acyl chain reduction in one chamber with acyl chain elongation in the other.
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