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9D49

Atomic model of triple mutant S. cerevisiae Fatty Acid Synthase (FAS) in complex with Palmitoyl-CoA (in vitro binding)

This is a non-PDB format compatible entry.
Summary for 9D49
Entry DOI10.2210/pdb9d49/pdb
EMDB information46554
DescriptorFatty acid synthase subunit beta, Fatty acid synthase subunit alpha, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
Functional Keywordspalmitoyl-coa, fas, allosteric inhibition, biosynthetic protein
Biological sourceSaccharomyces cerevisiae (brewer's yeast)
More
Total number of polymer chains12
Total formula weight2625522.50
Authors
Hasan, N.S.M.,Keszei, F.A.A.,Mazhab-Jafari, M.T. (deposition date: 2024-08-12, release date: 2025-08-27, Last modification date: 2025-10-15)
Primary citationHasan, S.M.N.,Samani, E.K.,Keszei, A.F.A.,Heydari, M.,Mazhab-Jafari, M.T.
Allosteric regulation of fungal fatty acid synthesis.
Structure, 2025
Cited by
PubMed Abstract: Mycobiota fatty acid synthases (FASs) catalyze iterative cycles of condensation, dehydration, and reduction to produce saturated fatty acids. Although these multienzymes are attractive antifungal drug targets, no clinically approved small-molecule inhibitors exist, and the regulation of de novo fatty acid synthesis remains poorly understood. Here, we identify an allosteric regulation of the FAS ketoacyl reduction reaction by palmitoyl-CoA. The palmitate moiety binds a distal site on the central wheel of fungal FAS from Saccharomyces cerevisiae and Candida albicans. This site also accommodates shorter acyl chains, but only palmitoyl-CoA suppresses ketoacyl reductase (KR) activity. While no major conformational changes occur in the reductase domain, palmitoyl-CoA binding quenches dynamics in the central disk, improving local resolution and stabilizing structured water molecules. This entropic effect underlies allosteric communication to the reductase site. Our findings uncover a regulatory mechanism of fungal FAS exploitable for antifungal drug design.
PubMed: 41043416
DOI: 10.1016/j.str.2025.09.005
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.65 Å)
Structure validation

243083

数据于2025-10-15公开中

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