ArticleScience advances2024
Structural basis for membrane association and catalysis by phosphatidylserine synthase in
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- 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
- Alternating High-Fat and Polysaccharide Diets Modulates Gut Phage-Bacterial Interplay.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- ConNIS and labeling instability: New statistical methods for improving the detection of essential genes in TraDIS libraries.PLoS computational biology · 2026Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatidylserine synthase (PssA) is essential in the biosynthesis of phosphatidylethanolamine, a major phospholipid of bacterial membranes. A peripheral membrane protein PssA can associate with the cellular membrane in its active state or exist in the cytosol in an inactive form. The membrane-bound enzyme acts on cytidine diphosphate diacylglycerol (CDP-DG) to form cytidine monophosphate and a covalent intermediate, which is subsequently targeted by serine to produce phosphatidylserine. Here, we present two crystal structures of
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