ArticleProceedings of the National Academy of Sciences of the United States of America2014
Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 66 citations in OpenAlex.
- The Legionella pneumophila effector SidL is an adenylyltransferase that modifies the glycolytic intermediate 3-phosphoglycerate.Molecular cell · 2026Article
- Structural basis of PLPP3-mediated lipid phosphate dephosphorylation and its role in melanoma.Nature communications · 2026Article
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Structural basis for the catalytic mechanism of human lipid phosphate phosphatases.Nature chemical biology · 2026Article
- RNAi-mediated knockdown of sphingomyelin synthase gene affects egg development and female fecundity in Panonychus citri (McGregor) (Acari: Tetranychidae).Experimental & applied acarology · 2026Article
- Structural insight into the glucose-6-phosphate transport by G6PT1 and inhibition mechanism of CGA.Science advances · 2026Article
- Analysis of the regulation of undecaprenyl diphosphate dephosphorylation in Escherichia coli.FEBS open bio · 2025Article
- The induced-fit and catalytic mechanisms of human G6PC1.Cell discovery · 2025Article
- Structural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics.Journal of the American Chemical Society · 2024Article
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology.Microbial cell factories · 2024Article
- Genetic characterization of multidrug-resistantFrontiers in cellular and infection microbiology · 2024Article
- Plasma membrane phospholipid phosphatase-related proteins as pleiotropic regulators of neuron growth and excitability.Frontiers in molecular neuroscience · 2022Review
- Towards discovery of inhibitors of the undecaprenyl-pyrophosphate phosphatase BacA by virtual high-throughput screening.Computational and structural biotechnology journal · 2022Article
- Pyrrolidine-based 3-deoxysphingosylphosphorylcholine analogs as possible candidates against neglected tropical diseases (NTDs): identification of hit compounds towards development of potential treatment ofJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Eugene P. Kennedy's Legacy: Defining Bacterial Phospholipid Pathways and Function.Frontiers in molecular biosciences · 2021Review
- The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface.Current research in structural biology · 2021Article
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Lipid Phosphate Phosphatases and Cancer.Biomolecules · 2020Review
- Involvement ofAntibiotics (Basel, Switzerland) · 2020Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-integrated type II phosphatidic acid phosphatases (PAP2s) are important for numerous bacterial to human biological processes, including glucose transport, lipid metabolism, and signaling. Escherichia coli phosphatidylglycerol-phosphate phosphatase B (ecPgpB) catalyzes removing the terminal phosphate group from a lipid carrier, undecaprenyl pyrophosphate, and is essential for transport of many hydrophilic small molecules across the membrane. We determined the crystal structure of ecPgpB at a resolution of 3.2 Å. This structure shares a similar folding topology and a nearly identical active site with soluble PAP2 enzymes. However, the substrate binding mechanism appears to be fundamentally different from that in soluble PAP2 enzymes. In ecPgpB, the potential substrate entrance to the active site is located in a cleft formed by a V-shaped transmembrane helix pair, allowing lateral movement of the lipid substrate entering the active site from the membrane lipid bilayer. Activity assays of point mutations confirmed the importance of the catalytic residues and potential residues involved in phosphate binding. The structure also suggests an induced-fit mechanism for the substrate binding. The 3D structure of ecPgpB serves as a prototype to study eukaryotic PAP2 enzymes, including human glucose-6-phosphatase, a key enzyme in the homeostatic regulation of blood glucose concentrations.
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