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Architecture of mammalian fatty acid synthase at 4.5 angstrom resolution
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 755159
Author(s) Maier, T.; Jenni, S.; Ban, N.
Author(s) at UniBasel Maier, Timm
Year 2006
Title Architecture of mammalian fatty acid synthase at 4.5 angstrom resolution
Journal Science
Volume 311
Number 5765
Pages / Article-Number 1258-1262
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.
Publisher American Association for the Advancement of Science
ISSN/ISBN 0036-8075 ; 1095-9203
edoc-URL http://edoc.unibas.ch/45834/
Full Text on edoc No
Digital Object Identifier DOI 10.1126/science.1123248
ISI-Number 000235870400033
Document type (ISI) article
 
   

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