ArticleBiochemistry2012
Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- "Just the Best Ones" combination: a new strategy for multi-epitope vaccine candidate based on immunoinformatics analysis to induce protective immunity against MRSA infection.Microbiology spectrum · 2026Article
- ImmobilizedFrontiers in bioengineering and biotechnology · 2025Article
- Thermally-triggered L-menthol release system based on starch sodium octenyl succinate/Nisin-stabilized high internal phase Pickering Emulsion: Development, characterization and meatball coating application.Current research in food science · 2025Article
- Review
- The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.Toxins · 2017Review
- Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion.The Journal of biological chemistry · 2015Article
- Gates of enzymes.Chemical reviews · 2013Review
- The cation-π box is a specific phosphatidylcholine membrane targeting motif.The Journal of biological chemistry · 2013Article
- Cation-π interactions as lipid-specific anchors for phosphatidylinositol-specific phospholipase C.Journal of the American Chemical Society · 2013Article
- Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding?Biophysical journal · 2013Article
- Competition between anion binding and dimerization modulates Staphylococcus aureus phosphatidylinositol-specific phospholipase C enzymatic activity.The Journal of biological chemistry · 2012Article
- Crystallization, optimization and preliminary X-ray characterization of a metal-dependent PI-PLC from Streptomyces antibioticus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Staphylococcus aureus secretes a phosphatidylinositol-specific phospholipase C (PI-PLC) as a virulence factor that is unusual in exhibiting higher activity at acidic pH values than other enzymes in this class. We have determined the crystal structure of this enzyme at pH 4.6 and pH 7.5. Under slightly basic conditions, the S. aureus PI-PLC structure closely follows the conformation of other bacterial PI-PLCs. However, when crystallized under acidic conditions, a large section of mobile loop at the αβ-barrel rim in the vicinity of the active site shows ~10 Å shift. This loop displacement at acidic pH is the result of a titratable intramolecular π-cation interaction between His258 and Phe249. This was verified by a structure of the mutant protein H258Y crystallized at pH 4.6, which does not exhibit the large loop shift. The intramolecular π-cation interaction for S. aureus PI-PLC provides an explanation for the activity of the enzyme at acid pH and also suggests how phosphatidylcholine, as a competitor for Phe249, may kinetically activate this enzyme.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.