Function
Stringent starvation protein A (SspA) is an RNA polymerase-associated protein involved in nucleotide metabolism acid tolerance and virulence of bacteria[1].
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.
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[2]. 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
