ArticleNature communications2017
Structural insights into the committed step of bacterial phospholipid biosynthesis.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
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- Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025Review
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- The Multifaceted Impact of Bioactive Lipids on Gut Health and Disease.International journal of molecular sciences · 2024Review
- PlsX and PlsY: Additional roles beyond glycerophospholipid synthesis in Gram-negative bacteria.mBio · 2024Article
- Structural insights into phosphatidylethanolamineScience advances · 2024Article
- Identifying Residues for Substrate Recognition in Human GPAT4 by Molecular Dynamics Simulations.International journal of molecular sciences · 2024Article
- Targeted Overexpression ofBiology · 2024Article
- Aminolipids in bacterial membranes and the natural environment.The ISME journal · 2024Review
- Mix-and-extrude: high-viscosity sample injection towards time-resolved protein crystallography.Journal of applied crystallography · 2023Article
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- Domain architecture and catalysis of the Staphylococcus aureus fatty acid kinase.The Journal of biological chemistry · 2022Article
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- A Novel Trehalose Synthase for the Production of Trehalose and Trehalulose.Microbiology spectrum · 2021Article
- Heat Adaptation Induced Cross Protection Against Ethanol Stress inFrontiers in microbiology · 2021Article
- The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface.Current research in structural biology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane-integral glycerol 3-phosphate (G3P) acyltransferase PlsY catalyses the committed and essential step in bacterial phospholipid biosynthesis by acylation of G3P, forming lysophosphatidic acid. It contains no known acyltransferase motifs, lacks eukaryotic homologs, and uses the unusual acyl-phosphate as acyl donor, as opposed to acyl-CoA or acyl-carrier protein for other acyltransferases. Previous studies have identified several PlsY inhibitors as potential antimicrobials. Here we determine the crystal structure of PlsY at 1.48 Å resolution, revealing a seven-transmembrane helix fold. Four additional substrate- and product-bound structures uncover the atomic details of its relatively inflexible active site. Structure and mutagenesis suggest a different acylation mechanism of 'substrate-assisted catalysis' that, unlike other acyltransferases, does not require a proteinaceous catalytic base to complete. The structure data and a high-throughput enzymatic assay developed in this work should prove useful for virtual and experimental screening of inhibitors against this vital bacterial enzyme.
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