4ae5

STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS

spinqualitylabelsall models 4ae5, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ae5 is a 4 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: FMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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