ArticleScientific reports2019
Electron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.Protein science : a publication of the Protein Society · 2026Article
- Decreased cytoplasmic crowding via inhibition of ribosome biogenesis can trigger Candida albicans filamentous growth.Nature microbiology · 2026Article
- HadBD dehydratase from Mycobacterium tuberculosis fatty acid synthase type II: A singular structure for a unique function.Protein science : a publication of the Protein Society · 2024Article
- Direct structural analysis of a single acyl carrier protein domain in fatty acid synthase from the fungus Saccharomyces cerevisiae.Communications biology · 2024Article
- Interface Engineering of Carrier-Protein-Dependent Metabolic Pathways.ACS chemical biology · 2023Article
- Identification of triazenyl indoles as inhibitors of fungal fatty acid biosynthesis with broad-spectrum activity.Cell chemical biology · 2023Article
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Article
- Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis.BMC biology · 2022Article
- Fatty Acid Synthase: Structure, Function, and Regulation.Sub-cellular biochemistry · 2022Review
- Article
- A GXThe Journal of biological chemistry · 2021Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
During fatty acid biosynthesis, acyl carrier proteins (ACPs) from type I fungal fatty acid synthase (FAS) shuttle substrates and intermediates within a reaction chamber that hosts multiple spatially-fixed catalytic centers. A major challenge in understanding the mechanism of ACP-mediated substrate shuttling is experimental observation of its transient interaction landscape within the reaction chamber. Here, we have shown that ACP spatial distribution is sensitive to the presence of substrates in a catalytically inhibited state, which enables high-resolution investigation of the ACP-dependent conformational transitions within the enoyl reductase (ER) reaction site. In two fungal FASs with distinct ACP localization, the shuttling domain is targeted to the ketoacyl-synthase (KS) domain and away from other catalytic centers, such as acetyl-transferase (AT) and ER domains by steric blockage of the KS active site followed by addition of substrates. These studies strongly suggest that acylation of phosphopantetheine arm of ACP may be an integral part of the substrate shuttling mechanism in type I fungal FAS.
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