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Architecture of a fungal fatty acid synthase at 5 angstrom resolution
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 755158
Author(s) Jenni, S.; Leibundgut, M.; Maier, T.; Ban, N.
Author(s) at UniBasel Maier, Timm
Year 2006
Title Architecture of a fungal fatty acid synthase at 5 angstrom resolution
Journal Science
Volume 311
Number 5765
Pages / Article-Number 1263-1267
Abstract All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha(6)beta(6) complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to similar to 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.
Publisher American Association for the Advancement of Science
ISSN/ISBN 0036-8075 ; 1095-9203
edoc-URL http://edoc.unibas.ch/45833/
Full Text on edoc No
Digital Object Identifier DOI 10.1126/science.1123251
ISI-Number 000235870400034
Document type (ISI) Article
 
   

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