ArticleNature structural & molecular biology2021
The structural basis of fatty acid elongation by the ELOVL elongases.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Phospholipase D2 acts upstream of PI4P 5-kinases in the response of neurons to extracellular viscosity.iScience · 2026Article
- Molecular basis of HACD-TECR complex mediated very-long-chain fatty acid elongation reveal a potential target in colorectal cancer.Science advances · 2026Article
- DietaryAnimals : an open access journal from MDPI · 2026Article
- Computational Analysis of ELOVL6 Structure and Inhibition for Rational Drug Design.Journal of chemical information and modeling · 2026Article
- Integrated genomic, transcriptomic, and metabolomic profile analysis reveals molecular mechanism underlying meat quality traits in Chinese Kangle chickens.Food chemistry. Molecular sciences · 2026Article
- A conserved ER protein prevents lipotoxicity by stimulating the key enzyme in glycerolipid synthesis.Nature communications · 2026Article
- Transcription factor 19 modulates fatty acid elongation and unfolded protein response to attenuate palmitic acid-induced hepatic dysfunction.Nature communications · 2026Article
- State-Level Organization of Spontaneous Behavior and Its Association with Plasma Fatty-Acid Profiles in Healthy Rats.Biology · 2026Article
- Fumarate hydratase ameliorates pressure overload induced cardiac remodeling by controlling Elovl7-mediated biosynthesis of unsaturated fatty acids.Acta pharmacologica Sinica · 2026Article
- Structural basis of VLCFA chain-length determination by the KCS6-CER2 complex in plants.Science advances · 2025Article
- Molecular basis of very-long-chain fatty acid elongation by the CER6-GL2 enzyme complex in plant wax biosynthesis.Science advances · 2025Article
- Biallelic ELOVL1 Variants Are Linked to Hypomyelinating Leukodystrophy, Movement Disorder, and Ichthyosis.Movement disorders : official journal of the Movement Disorder Society · 2025Article
- Proteomic Ligandability Maps of Phosphorus(V) Stereoprobes Identify Covalent TLCD1 Inhibitors.Journal of the American Chemical Society · 2025Article
- Engineering yeast for tailored fatty acid profiles.Applied microbiology and biotechnology · 2025Review
- Structural basis of the mechanism and inhibition of a human ceramide synthase.Nature structural & molecular biology · 2025Article
- Proteomic Ligandability Maps of Phosphorus(V) Stereoprobes Identify Covalent TLCD1 Inhibitors.bioRxiv : the preprint server for biology · 2025Article
- Ketogenesis supports hepatic polyunsaturated fatty acid homeostasis via fatty acid elongation.Science advances · 2025Article
- In silico characterization of Rhodotorula toruloides ELO-like elongases and production of very-long-chain fatty acids by expressing Rtelo2, RtKCR, RtHCD, and RtECR through IRES-mediated bicistrons.World journal of microbiology & biotechnology · 2024Article
- Article
- Structural and functional analysis of plant ELO-like elongase for fatty acid elongation.Plant molecular biology · 2024Article
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16 authors.
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Abstract
Very long chain fatty acids (VLCFAs) are essential building blocks for the synthesis of ceramides and sphingolipids. The first step in the fatty acid elongation cycle is catalyzed by the 3-keto acyl-coenzyme A (CoA) synthases (in mammals, ELOVL elongases). Although ELOVLs are implicated in common diseases, including insulin resistance, hepatic steatosis and Parkinson's, their underlying molecular mechanisms are unknown. Here we report the structure of the human ELOVL7 elongase, which comprises an inverted transmembrane barrel surrounding a 35-Å long tunnel containing a covalently attached product analogue. The structure reveals the substrate-binding sites in the narrow tunnel and an active site deep in the membrane. We demonstrate that chain elongation proceeds via an acyl-enzyme intermediate involving the second histidine in the canonical HxxHH motif. The unusual substrate-binding arrangement and chemistry suggest mechanisms for selective ELOVL inhibition, relevant for diseases where VLCFAs accumulate, such as X-linked adrenoleukodystrophy.
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