4V59
Crystal structure of fatty acid synthase complexed with nadp+ from thermomyces lanuginosus at 3.1 angstrom resolution.
This is a non-PDB format compatible entry.
Summary for 4V59
| Entry DOI | 10.2210/pdb4v59/pdb |
| Descriptor | FATTY ACID SYNTHASE ALPHA SUBUNITS, FATTY ACID SYNTHASE BETA SUBUNITS, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | fungal, dehydratase, enoyl reductase, ketoacyl synthase, ketoacyl reductase, malonyl/palmitoyl transferase, transferase, substrate shuttling, multifunctional enzyme, acyl carrier protein, fatty acid synthesis, acetyl transferase, fatty acid synthase |
| Biological source | THERMOMYCES LANUGINOSUS More |
| Total number of polymer chains | 12 |
| Total formula weight | 2632545.46 |
| Authors | Jenni, S.,Leibundgut, M.,Boehringer, D.,Frick, C.,Mikolasek, B.,Ban, N. (deposition date: 2007-03-09, release date: 2014-07-09, Last modification date: 2024-05-08) |
| Primary citation | Jenni, S.,Leibundgut, M.,Boehringer, D.,Frick, C.,Mikolasek, B.,Ban, N. Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling Science, 316:254-, 2007 Cited by 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 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. PubMed: 17431175DOI: 10.1126/SCIENCE.1138248 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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