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|2uva, resolution 3.10Å ()|
CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400
We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.
Structure of fungal fatty acid synthase and implications for iterative substrate shuttling., Jenni S, Leibundgut M, Boehringer D, Frick C, Mikolasek B, Ban N, Science. 2007 Apr 13;316(5822):254-61. PMID:17431175
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.