Stringent starvation protein
FunctionStringent 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. RelevanceTularemia caused by the pathogen Francisella tularensis may be treated by inhibitors of SspA-MglA regulators. Structural highlightsThe 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 |
| ||||||||||
ReferencesReferences
- ↑ Wang F, Shi J, He D, Tong B, Zhang C, Wen A, Zhang Y, Feng Y, Lin W. Structural basis for transcription inhibition by E. coli SspA. Nucleic Acids Res. 2020 Sep 25;48(17):9931-9942. doi: 10.1093/nar/gkaa672. PMID:32785630 doi:http://dx.doi.org/10.1093/nar/gkaa672
- ↑ Cuthbert BJ, Ross W, Rohlfing AE, Dove SL, Gourse RL, Brennan RG, Schumacher MA. Dissection of the molecular circuitry controlling virulence in Francisella tularensis. Genes Dev. 2017 Aug 1;31(15):1549-1560. doi: 10.1101/gad.303701.117. Epub 2017, Sep 1. PMID:28864445 doi:http://dx.doi.org/10.1101/gad.303701.117