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STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESISSTRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS
Structural highlights
FunctionTRAP_STAA8 Signal transduction protein, which is a major regulator of staphylococcal pathogenesis. Phosphorylated TRAP leads to the activation of agr system and consequent RNAIII synthesis resulting in the expression of several virulence factors. Up-regulates the expression of most toxins and genes known to be necessary for biofilm formation.[1] [2] Publication Abstract from PubMedThe crystal structure of the signal transduction protein TRAP is reported at 1.85 A resolution. The structure of TRAP consists of a central eight-stranded beta-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit. Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).,Henrick K, Hirshberg M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):744-50., Epub 2012 Jun 22. PMID:22750855[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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