2UV8

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

Summary for 2UV8

• Entry DOI: 10.2210/pdb2uv8/pdb
• Descriptor: FATTY ACID SYNTHASE SUBUNIT ALPHA (FAS2), FATTY ACID SYNTHASE SUBUNIT BETA (FAS1), FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: fatty acid biosynthesis, malonyl/palmitoyl transferase, phosphopantetheine, fatty acid synthase, transferase, oxidoreductase, lipid synthesis, substrate shuttling, acyl carrier protein, ketoacyl reductase, acetyl transferase, enoyl reductase, phosphorylation, ketoacyl synthase, fatty acid synthesis, multifunctional enzyme, nad, nadp, lyase, yeast, hydrolase, dehydratase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 6
• Total formula weight: 1310370.80

Authors

Leibundgut, M.,Jenni, S.,Frick, C.,Ban, N. (deposition date: 2007-03-09, release date: 2007-04-17, Last modification date: 2023-12-13)

Primary citation

Leibundgut, M.,Jenni, S.,Frick, C.,Ban, N.
Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase
Science, 316:288-, 2007

PubMed Abstract: In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.

PubMed: 17431182
DOI: 10.1126/SCIENCE.1138249

Experimental method

X-RAY DIFFRACTION (3.1 Å)