5u51

Structure of Francisella tularensis heterodimeric SspA (MglA-SspA) in complex with ppGpp

spinqualitylabelsall models 5u51, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u51 is a 4 chain structure with sequence from Francisella tularensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: 1PE, G4P, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5NHJ6_FRATT Publication Abstract from PubMed Francisella tularensis, the etiological agent of tularemia, is one of the most infectious bacteria known. Because of its extreme pathogenicity, F. tularensis is classified as a category A bioweapon by the US government. F. tularensis virulence stems from genes encoded on the Francisella pathogenicity island (FPI). An unusual set of Francisella regulators-the heteromeric macrophage growth locus protein A (MglA)-stringent starvation protein A (SspA) complex and the DNA-binding protein pathogenicity island gene regulator (PigR)-activates FPI transcription and thus is essential for virulence. Intriguingly, the second messenger, guanosine-tetraphosphate (ppGpp), which is produced during infection, is also involved in coordinating Francisella virulence; however, its role has been unclear. Here we identify MglA-SspA as a novel ppGpp-binding complex and describe structures of apo- and ppGpp-bound MglA-SspA. We demonstrate that MglA-SspA, which binds RNA polymerase (RNAP), also interacts with the C-terminal domain of PigR, thus anchoring the (MglA-SspA)-RNAP complex to the FPI promoter. Furthermore, we show that MglA-SspA must be bound to ppGpp to mediate high-affinity interactions with PigR. Thus, these studies unveil a novel pathway different from those described previously for regulation of transcription by ppGpp. The data also indicate that F. tularensis pathogenesis is controlled by a highly interconnected molecular circuitry in which the virulence machinery directly senses infection via a small molecule stress signal. Dissection of the molecular circuitry controlling virulence in Francisella tularensis.,Cuthbert BJ, Ross W, Rohlfing AE, Dove SL, Gourse RL, Brennan RG, Schumacher MA Genes Dev. 2017 Aug 1;31(15):1549-1560. doi: 10.1101/gad.303701.117. Epub 2017, Sep 1. PMID:28864445 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Stringent starvation protein Stringent starvation protein 3D structures

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