Architecture of mammalian fatty acid synthase at 4.5 angstrom resolution

Maier, T. and Jenni, S. and Ban, N.. (2006) Architecture of mammalian fatty acid synthase at 4.5 angstrom resolution. Science, 311 (5765). pp. 1258-1262.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/45834/

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:27 Nov 2017 12:20
Deposited On:27 Nov 2017 12:20

Repository Staff Only: item control page