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- W2051250777 endingPage "1267" @default.
- W2051250777 startingPage "1263" @default.
- W2051250777 abstract "All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton α 6 β 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 ∼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." @default.
- W2051250777 created "2016-06-24" @default.
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- W2051250777 creator A5073528182 @default.
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- W2051250777 date "2006-03-03" @default.
- W2051250777 modified "2023-09-23" @default.
- W2051250777 title "Architecture of a Fungal Fatty Acid Synthase at 5 Å Resolution" @default.
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- W2051250777 doi "https://doi.org/10.1126/science.1123251" @default.
- W2051250777 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16513976" @default.
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