ArticleThe Journal of biological chemistry2015
Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 59 citations in OpenAlex.
- The serine-rich C-terminal tail of the Listeria monocytogenes secretion chaperone PrsA2 is critical for bacterial virulence and resistance to cell-wall active antibiotics.PLoS pathogens · 2026Article
- The roles of theJournal of bacteriology · 2026Article
- Ag-Decorated Hydrogen Molybdenum Bronze Nanotubes as Dual-Action Agents AgainstBioinorganic chemistry and applications · 2026Article
- High-Level Expression of Humicola insolens Cutinase in Bacillus subtilis.Applied biochemistry and biotechnology · 2025Article
- Crystal structure and biophysical characterisation of the enterococcal foldase PpiC, a cross-opsonic antigen against gram-positive nosocomial pathogens.The FEBS journal · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions.mSphere · 2025Article
- A widespread and ancient bacterial machinery assembles cytochrome OmcS nanowires essential for extracellular electron transfer.Cell chemical biology · 2025Article
- Investigation of cross-opsonic effect leads to the discovery of PPIase-domain containing protein vaccine candidate to prevent infections by Gram-positive ESKAPE pathogens.BMC microbiology · 2024Article
- The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O duringmBio · 2024Article
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Article
- Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome.Nature microbiology · 2024Article
- TerC proteins function during protein secretion to metalate exoenzymes.Nature communications · 2023Article
- Enhanced Cell Wall and Cell Membrane Activity Promotes Heat Adaptation ofInternational journal of molecular sciences · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.Research square · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.bioRxiv : the preprint server for biology · 2023Article
- Molecular docking analysis of juglone with parvulin-type PPiase PrsA fromBioinformation · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretion of proteins into the membrane-cell wall space is essential for cell wall biosynthesis and pathogenicity in Gram-positive bacteria. Folding and maturation of many secreted proteins depend on a single extracellular foldase, the PrsA protein. PrsA is a 30-kDa protein, lipid anchored to the outer leaflet of the cell membrane. The crystal structure of Bacillus subtilis PrsA reveals a central catalytic parvulin-type prolyl isomerase domain, which is inserted into a larger composite NC domain formed by the N- and C-terminal regions. This domain architecture resembles, despite a lack of sequence conservation, both trigger factor, a ribosome-binding bacterial chaperone, and SurA, a periplasmic chaperone in Gram-negative bacteria. Two main structural differences are observed in that the N-terminal arm of PrsA is substantially shortened relative to the trigger factor and SurA and in that PrsA is found to dimerize in a unique fashion via its NC domain. Dimerization leads to a large, bowl-shaped crevice, which might be involved in vivo in protecting substrate proteins from aggregation. NMR experiments reveal a direct, dynamic interaction of both the parvulin and the NC domain with secretion propeptides, which have been implicated in substrate targeting to PrsA.
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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.