2CDH

ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.

Summary for 2CDH

• Entry DOI: 10.2210/pdb2cdh/pdb
• Descriptor: ENOYL REDUCTASE, MALONYL/PALMITOYL TRANSFERASE, KETOACYL SYNTHASE, ... (5 entities in total)
• Functional Keywords: transferase, fatty acid synthesis, multifunctional enzyme, fungal fatty acid synthase
• Biological source: THERMOMYCES LANUGINOSUS; More
• Total number of polymer chains: 36
• Total formula weight: 1091944.14

Authors

Jenni, S.,Leibundgut, M.,Maier, T.,Ban, N. (deposition date: 2006-01-24, release date: 2006-03-07, Last modification date: 2024-02-14)

Primary citation

Jenni, S.,Leibundgut, M.,Maier, T.,Ban, N.
Architecture of a Fungal Fatty Acid Synthase at 5 A Resolution.
Science, 311:1263-, 2006

PubMed Abstract: All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 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 approximately 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.

PubMed: 16513976
DOI: 10.1126/SCIENCE.1123251

Experimental method

X-RAY DIFFRACTION (4.2 Å)