ArticleThe Journal of biological chemistry2015
The Crystal Structure of an Integral Membrane Fatty Acid α-Hydroxylase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 63 citations in OpenAlex.
- The algal homolog of the plant CER1 and CER3 proteins is a bifunctional hydrocarbon-forming enzyme.The New phytologist · 2026Article
- Clinical, Radiological, and Genetic Profile of Patients withTremor and other hyperkinetic movements (New York, N.Y.) · 2026Review
- Sterol-C4-methyl-oxidase Erg251 governs Candida albicans hypoxic growth, commensalism and virulence.Nature communications · 2025Article
- Genome-wide analysis and functional validation of the cotton FAH gene family for salt stress.BMC genomics · 2025Article
- No Bridge between Us: EXAFS and Computations Confirm Two Distant Iron Ions Comprise the Active Site of Alkane Monooxygenase (AlkB).Journal of the American Chemical Society · 2025Article
- Insights into Heterocycle Biosynthesis in the Cytotoxic Polyketide Alkaloid Janustatin A from a Plant-Associated Bacterium.Biochemistry · 2025Article
- 2-Hydroxylation is a chemical switch linking fatty acids to glucose-stimulated insulin secretion.The Journal of biological chemistry · 2024Article
- Broad Chain-Length Specificity of the Alkane-Forming Enzymes NoCER1A and NoCER3A/B in Nymphaea odorata.Plant & cell physiology · 2024Article
- Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Review of Eukaryote Cellular Membrane Lipid Composition, with Special Attention to the Fatty Acids.International journal of molecular sciences · 2023Review
- Lactate dehydrogenase D is a general dehydrogenase for D-2-hydroxyacids and is associated with D-lactic acidosis.Nature communications · 2023Article
- Dynamic Interplay between Social Brain Development and Nutrient Intake in Young Children.Nutrients · 2023Article
- Structure and mechanism of the alkane-oxidizing enzyme AlkB.Nature communications · 2023Article
- Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1.bioRxiv : the preprint server for biology · 2023Article
- Fatty Acid 2-Hydroxylase and 2-Hydroxylated Sphingolipids: Metabolism and Function in Health and Diseases.International journal of molecular sciences · 2023Review
- Elucidation of sterol biosynthesis pathway and its co-regulation with fatty acid biosynthesis in the oleaginous marine protistFrontiers in bioengineering and biotechnology · 2023Article
- Membrane fatty acid desaturase: biosynthesis, mechanism, and architecture.Applied microbiology and biotechnology · 2022Review
- Age-Dependent Increase in Schmidt-Lanterman Incisures and a Cadm4-Associated Membrane Skeletal Complex in Fatty Acid 2-hydroxylase Deficient Mice: a Mouse Model of Spastic Paraplegia SPG35.Molecular neurobiology · 2022Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Neuronal electrical impulse propagation is facilitated by the myelin sheath, a compact membrane surrounding the axon. The myelin sheath is highly enriched in galactosylceramide (GalCer) and its sulfated derivative sulfatide. Over 50% of GalCer and sulfatide in myelin is hydroxylated by the integral membrane enzyme fatty acid 2-hydroxylase (FA2H). GalCer hydroxylation contributes to the compact nature of the myelin membrane, and mutations in FA2H result in debilitating leukodystrophies and spastic paraparesis. We report here the 2.6 Å crystal structure of sphingolipid α-hydroxylase (Scs7p), a yeast homolog of FA2H. The Scs7p core is composed of a helical catalytic cap domain that sits atop four transmembrane helices that anchor the enzyme in the endoplasmic reticulum. The structure contains two zinc atoms coordinated by the side chains of 10 highly conserved histidines within a dimetal center located near the plane of the cytosolic membrane. We used a yeast genetic approach to confirm the important role of the dimetal-binding histidines in catalysis and identified Tyr-322 and Asp-323 as critical determinants involved in the hydroxylase reaction. Examination of the Scs7p structure, coupled with molecular dynamics simulations, allowed for the generation of a model of ceramide binding to Scs7p. Comparison of the Scs7p structure and substrate-binding model to the structure of steroyl-CoA desaturase revealed significant differences in the architecture of the catalytic cap domain and location of the dimetal centers with respect to the membrane. These observations provide insight into the different mechanisms of substrate binding and recognition of substrates by the hydroxylase and desaturase enzymes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.