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Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase
Marc Leibundgut, Simon Jenni, Christian Frick and Nenad Ban
New Series, Vol. 316, No. 5822 (Apr. 13, 2007), pp. 288-290
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/20036016
Page Count: 3
You can always find the topics here!Topics: Yeasts, Active sites, Enzymes, Prosthetics, Fatty acids, Enzyme substrates, Electron density, Wheels, Biochemistry, Carrier proteins
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In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.
Science © 2007 American Association for the Advancement of Science