ArticleScientific reports2021
Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Structural basis of substrate recognition and membrane association by the bacterial lysyl-phosphatidylglycerol hydrolase AcvB.Communications biology · 2026Article
- The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026Review
- Polyethylene Mulch Emissions Differentially Impact the Soil Metabolome and Microbial Community in Field Pea (Journal of xenobiotics · 2026Article
- Identification of regulatory candidate genes for Lentinula edodes pileus development based on transcriptome analysis.G3 (Bethesda, Md.) · 2026Article
- Model Lipid Bilayers as Platforms for Replicating Bacterial Membranes: A Study of Dynamics and Structural Heterogeneity.The journal of physical chemistry. B · 2026Article
- Self-Stabilizing Covalent Ligand Targets Bacterial Phosphatidylethanolamine and Enhances Antibiotic Efficacy.Pharmaceutics · 2026Article
- Origin and evolution of mitochondrial inner membrane composition.Journal of cell science · 2025Review
- Structural basis for psilocybin biosynthesis.Nature communications · 2025Article
- Effects of surfactin stress on gene expression and pathological changes in Spodoptera litura.Scientific reports · 2024Article
- Structural insights into phosphatidylethanolamineScience advances · 2024Article
- Ethanolamine metabolism through two genetically distinct loci enables Klebsiella pneumoniae to bypass nutritional competition in the gut.PLoS pathogens · 2024Article
- Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights.Journal of fungi (Basel, Switzerland) · 2024Review
- Structural biology of MCR-1-mediated resistance to polymyxin antibiotics.Current opinion in structural biology · 2023Review
- Effects of Trehalose Supplementation on Lipid Composition of Rooster Spermatozoa Membranes in a Freeze/Thaw Protocol.Animals : an open access journal from MDPI · 2023Article
- Metabolomics reveals the mechanism of action of meropenem and amikacin combined in the treatment ofFrontiers in cellular and infection microbiology · 2023Article
- Egg yolk lipids: separation, characterization, and utilization.Food science and biotechnology · 2022Review
- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- An evolutionary conserved detoxification system for membrane lipid-derived peroxyl radicals in Gram-negative bacteria.PLoS biology · 2022Article
- Discovery of Potent and Selective Inhibitors against Protein-Derived Electrophilic Cofactors.Journal of the American Chemical Society · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatidylethanolamine (PE), a major component of the cellular membrane across all domains of life, is synthesized exclusively by membrane-anchored phosphatidylserine decarboxylase (PSD) in most bacteria. The enzyme undergoes auto-cleavage for activation and utilizes the pyruvoyl moiety to form a Schiff base intermediate with PS to facilitate decarboxylation. However, the structural basis for self-maturation, PS binding, and decarboxylation processes directed by PSD remain unclear. Here, we present X-ray crystal structures of PSD from Escherichia coli, representing an apo form and a PE-bound complex, in which the phospholipid is chemically conjugated to the essential pyruvoyl residue, mimicking the Schiff base intermediate. The high-resolution structures of PE-complexed PSD clearly illustrate extensive hydrophobic interactions with the fatty acyl chains of the phospholipid, providing insights into the broad specificity of the enzyme over a wide range of cellular PS. Furthermore, these structures strongly advocate the unique topology of the enzyme in a lipid bilayer environment, where the enzyme associates with cell membranes in a monotopic fashion via the N-terminal domain composed of three amphipathic helices. Lastly, mutagenesis analyses reveal that E. coli PSD primarily employs D90/D142-H144-S254 to achieve auto-cleavage for the proenzyme maturation, where D90 and D142 act in complementary to each other.
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