Structural highlights
Function
TRAP_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 PubMed
The 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
- ↑ Balaban N, Goldkorn T, Gov Y, Hirshberg M, Koyfman N, Matthews HR, Nhan RT, Singh B, Uziel O. Regulation of Staphylococcus aureus pathogenesis via target of RNAIII-activating Protein (TRAP). J Biol Chem. 2001 Jan 26;276(4):2658-67. PMID:11160124 doi:10.1074/jbc.m005446200
- ↑ Korem M, Gov Y, Kiran MD, Balaban N. Transcriptional profiling of target of RNAIII-activating protein, a master regulator of staphylococcal virulence. Infect Immun. 2005 Oct;73(10):6220-8. PMID:16177293 doi:10.1128/IAI.73.10.6220-6228.2005
- ↑ Henrick K, Hirshberg M. Structure of the signal transduction protein TRAP (target of RNAIII-activating protein). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):744-50., Epub 2012 Jun 22. PMID:22750855 doi:10.1107/S1744309112020167
