Stringent starvation protein: Difference between revisions

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'''Stringent starvation protein''' A (SspA) is an RNA polymerase-associated protein involved in nucleotide metabolism acid tolerance and virulence of bacteria<ref>PMID:32785630</ref>.
'''Stringent starvation protein''' A (SspA) is an RNA polymerase-associated protein involved in nucleotide metabolism acid tolerance and virulence of bacteria<ref>PMID:32785630</ref>.
In ''Francisella'' virulence, a set of regulators are essensial for its activation.  These regulators include the heterdimer of SspA, macrophage growth locus A (MglA) and pathogenicity island gene regulator (PigR).  The guanosine-tetraphosphate (ppGpp) is also involved in coordinating the virulence.  
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.  
== Disease =s


== Relevance ==
== Relevance ==
Tularemia caused by the pathogen ''Francisella tularensis'' may be treated by inhibitors of SspA-MglA regulators.


== Structural highlights ==
== Structural highlights ==


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
The 3D structure of the complex of SspA and MglA shows a heterodimer with favourable interactions between the two molecules<ref>PMID:18864445</ref>.  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]]
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

Revision as of 11:50, 24 July 2022


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

SspA (pink, yellow) complex with MglA (green, grey), ppGpp, glycerol, PEG400 (PDB ID 5u51)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ SHANKS J. Subjective and objective noises in the ear. Med Rec (Reading). 1948 May;161(5):289-92. PMID:18864445

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Michal Harel, Alexander Berchansky
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