Stringent starvation protein

spinqualitylabelsall models SspA (deep sky blue) complex with MglA (pink), ppGpp, glycerol, PEG400 (PDB ID 5u51) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Stringent starvation protein A (SspA) is an RNA polymerase-associated protein involved in nucleotide metabolism, acid tolerance and virulence of bacteria. In Francisella virulence, a set of regulators are essensial for its activation. These regulators include the heterodimer of SspA, macrophage growth locus A (MglA) and pathogenicity island gene regulator (PigR). The guanosine-tetraphosphate (ppGpp) is also involved in coordinating the virulence. Stringent starvation protein B (SspB) binds to residues in the tag of tmRNA proteins marking them for degradation . Relevance Tularemia caused by the pathogen Francisella tularensis may be treated by inhibitors of SspA-MglA regulators. Structural highlights The 3D structure of the complex of SspA and MglA shows a heterodimer with favourable interactions between the two molecules. The ppGpp molecule binds to the open face of the SspA-MglA heterodimer interacting with both molecules. 3D structures of stringent starvation protein Stringent starvation protein 3D structures

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Michal Harel, Alexander Berchansky