ArticleBMC structural biology2009
Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.
Article in BMC structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- The roles of theJournal of bacteriology · 2026Article
- Characterization of antigen adjuvant interactions in polyacrylate adjuvanted vaccines.Biochemistry and biophysics reports · 2023Article
- Molecular docking analysis of juglone with parvulin-type PPiase PrsA fromBioinformation · 2023Article
- Lipoproteins in Gram-Positive Bacteria: Abundance, Function, Fitness.Frontiers in microbiology · 2020Review
- Coarse-grain simulations on NMR conformational ensembles highlight functional residues in proteins.Journal of the Royal Society, Interface · 2019Article
- Article
- Structural Analysis of the 42 kDa Parvulin ofBiomolecules · 2019Article
- PleiotropicFrontiers in pharmacology · 2019Article
- Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases.Scientific reports · 2017Article
- An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.Journal of bacteriology · 2017Article
- NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.BMC biology · 2016Article
- Evaluation of Staphylococcus aureus Lipoproteins: Role in Nutritional Acquisition and Pathogenicity.Frontiers in microbiology · 2016Article
- The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A.Antimicrobial agents and chemotherapy · 2015Article
- Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone.Infection and immunity · 2015Article
- Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules · 2015Review
- Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Journal of biological chemistry · 2015Article
- Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Microbiology and molecular biology reviews : MMBR · 2014Review
- Listeria monocytogenes virulence factor secretion: don't leave the cell without a chaperone.Frontiers in cellular and infection microbiology · 2014Review
- Mechanism of action of the arylomycin antibiotics and effects of signal peptidase I inhibition.Antimicrobial agents and chemotherapy · 2012Article
- A mutation in the PP2C phosphatase gene in a Staphylococcus aureus USA300 clinical isolate with reduced susceptibility to vancomycin and daptomycin.Antimicrobial agents and chemotherapy · 2012Article
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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
backgroundStaphylococcus aureus is a Gram-positive pathogenic bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. Recent emergence of S. aureus strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. S. aureus PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a parvulin-type peptidyl-prolyl cis-trans isomerase domain. PrsA is known to act as an essential folding factor for secreted proteins in Gram-positive bacteria and thus it is a potential target for antimicrobial drugs against S. aureus.
resultsWe have solved a high-resolution solution structure of the parvulin-type peptidyl-prolyl cis-trans isomerase domain of S. aureus PrsA (PrsA-PPIase). The results of substrate peptide titrations pinpoint the active site and demonstrate the substrate preference of the enzyme. With detailed NMR spectroscopic investigation of the orientation and tautomeric state of the active site histidines we are able to give further insight into the structure of the catalytic site. NMR relaxation analysis gives information on the dynamic behaviour of PrsA-PPIase.
conclusionDetailed structural description of the S. aureus PrsA-PPIase lays the foundation for structure-based design of enzyme inhibitors. The structure resembles hPin1-type parvulins both structurally and regarding substrate preference. Even though a wealth of structural data is available on parvulins, the catalytic mechanism has yet to be resolved. The structure of S. aureus PrsA-PPIase and our findings on the role of the conserved active site histidines help in designing further experiments to solve the detailed catalytic mechanism.
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