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• W2109463793 abstract "Sortase enzymes are vitally important for the virulence of gram-positive bacteria as they play a key role in the attachment of surface proteins to the cell wall. These enzymes recognize a specific sorting sequence in proteins destined to be displayed on the surface of the bacteria and catalyze the transpeptidation reaction that links it to a cell wall precursor molecule. Because of their role in establishing pathogenicity, and in light of the recent rise of antibiotic-resistant bacterial strains, sortase enzymes are novel drug targets. Here, we present a study of the prototypical sortase protein Staphylococcus aureus Sortase A (SrtA). Both conventional and accelerated molecular dynamics simulations of S. aureus SrtA in its apo state and when bound to an LPATG sorting signal (SS) were performed. Results support a binding mechanism that may be characterized as conformational selection followed by induced fit. Additionally, the SS was found to adopt multiple metastable states, thus resolving discrepancies between binding conformations in previously reported experimental structures. Finally, correlation analysis reveals that the SS actively affects allosteric pathways throughout the protein that connect the first and the second substrate binding sites, which are proposed to be located on opposing faces of the protein. Overall, these calculations shed new light on the role of dynamics in the binding mechanism and function of sortase enzymes." @default.
• W2109463793 created "2016-06-24" @default.
• W2109463793 creator A5007715260 @default.
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• W2109463793 date "2012-11-26" @default.
• W2109463793 modified "2023-09-24" @default.
• W2109463793 title "The binding mechanism, multiple binding modes, and allosteric regulation ofStaphylococcus aureusSortase A probed by molecular dynamics simulations" @default.
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• W2109463793 doi "https://doi.org/10.1002/pro.2168" @default.
• W2109463793 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3575916" @default.
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• W2109463793 hasPublicationYear "2012" @default.
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