2CF2

Architecture of mammalian fatty acid synthase

Summary for 2CF2

• Entry DOI: 10.2210/pdb2cf2/pdb
• Related: 2CDH
• Descriptor: FATTY ACID SYNTHASE, KS DOMAIN, FATTY ACID SYNTHASE, MAT DOMAIN, FATTY ACID SYNTHASE, DH DOMAIN, ... (5 entities in total)
• Functional Keywords: transferase, fatty acid metabolism, fatty acid biosynthesis, multienzyme
• Biological source: SUS SCROFA (PIG); More
• Total number of polymer chains: 10
• Total formula weight: 333132.67

Authors

Maier, T.,Jenni, S.,Ban, N. (deposition date: 2006-02-14, release date: 2006-03-07, Last modification date: 2024-05-08)

Primary citation

Maier, T.,Jenni, S.,Ban, N.
Architecture of Mammalian Fatty Acid Synthase at 4.5 A Resolution.
Science, 311:1258-, 2006

PubMed Abstract: The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.

PubMed: 16513975
DOI: 10.1126/SCIENCE.1123248

Experimental method

X-RAY DIFFRACTION (4.3 Å)