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-Structure paper
Title | Structure of fungal fatty acid synthase and implications for iterative substrate shuttling. |
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Journal, issue, pages | Science, Vol. 316, Issue 5822, Page 254-261, Year 2007 |
Publish date | Apr 13, 2007 |
Authors | Simon Jenni / Marc Leibundgut / Daniel Boehringer / Christian Frick / Bohdan Mikolásek / Nenad Ban / |
PubMed Abstract | 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 ...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. |
External links | Science / PubMed:17431175 |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.1 - 15.0 Å |
Structure data | EMDB-1338: PDB-4v58: PDB-4v59: |
Chemicals | ChemComp-FMN: ChemComp-NAP: |
Source |
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Keywords | TRANSFERASE / FUNGAL / DEHYDRATASE / ENOYL REDUCTASE / KETOACYL SYNTHASE / KETOACYL REDUCTASE / MALONYL/PALMITOYL TRANSFERASE / SUBSTRATE SHUTTLING / MULTIFUNCTIONAL ENZYME / ACYL CARRIER PROTEIN / FATTY ACID SYNTHESIS / ACETYL TRANSFERASE / FATTY ACID SYNTHASE |