Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 13 April 2007:
Vol. 316. no. 5822, pp. 254 - 261
DOI: 10.1126/science.1138248
Prev | Table of Contents | Next

Research Articles

Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling

Simon Jenni,* Marc Leibundgut,* Daniel Boehringer, Christian Frick, Bohdan Mikolásek, Nenad Ban{dagger}

We report crystal structures of the 2.6-megadalton {alpha}6ß6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The {alpha} and ß 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.

Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed E-mail: ban{at}mol.biol.ethz.ch

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Dynamics Simulations of the Apo-, Holo-, and Acyl-forms of Escherichia coli Acyl Carrier Protein.
D. I. Chan, T. Stockner, D. P. Tieleman, and H. J. Vogel (2008)
J. Biol. Chem. 283, 33620-33629
   Abstract »    Full Text »    PDF »
Crystal Structure of DltA: IMPLICATIONS FOR THE REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE ADENYLATION DOMAINS.
H. Yonus, P. Neumann, S. Zimmermann, J. J. May, M. A. Marahiel, and M. T. Stubbs (2008)
J. Biol. Chem. 283, 32484-32491
   Abstract »    Full Text »    PDF »
The Crystal Structure of a Mammalian Fatty Acid Synthase.
T. Maier, M. Leibundgut, and N. Ban (2008)
Science 321, 1315-1322
   Abstract »    Full Text »    PDF »
Inhibition of the fungal fatty acid synthase type I multienzyme complex.
P. Johansson, B. Wiltschi, P. Kumari, B. Kessler, C. Vonrhein, J. Vonck, D. Oesterhelt, and M. Grininger (2008)
PNAS 105, 12803-12808
   Abstract »    Full Text »    PDF »
Direct transfer of starter substrates from type I fatty acid synthase to type III polyketide synthases in phenolic lipid synthesis.
A. Miyanaga, N. Funa, T. Awakawa, and S. Horinouchi (2008)
PNAS 105, 871-876
   Abstract »    Full Text »    PDF »
Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase.
M. Leibundgut, S. Jenni, C. Frick, and N. Ban (2007)
Science 316, 288-290
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)