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6XZ5

RovC - regulator of virulence interconnected with the Csr system

Summary for 6XZ5
Entry DOI10.2210/pdb6xz5/pdb
DescriptorUncharacterized protein,RovC,Uncharacterized protein, SULFATE ION (3 entities in total)
Functional Keywordstranscriptional activator, type vi secretion, hexameric ring, regulator of virulence, dna binding protein
Biological sourceYersinia pseudotuberculosis serotype O:3 (strain YPIII)
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Total number of polymer chains1
Total formula weight28669.74
Authors
Sadana, P.,Scrima, A. (deposition date: 2020-02-02, release date: 2020-09-16, Last modification date: 2024-05-15)
Primary citationKnittel, V.,Sadana, P.,Seekircher, S.,Stolle, A.S.,Korner, B.,Volk, M.,Jeffries, C.M.,Svergun, D.I.,Heroven, A.K.,Scrima, A.,Dersch, P.
RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression.
Plos Pathog., 16:e1008552-e1008552, 2020
Cited by
PubMed Abstract: Type VI secretion systems (T6SSs) are complex macromolecular injection machines which are widespread in Gram-negative bacteria. They are involved in host-cell interactions and pathogenesis, required to eliminate competing bacteria, or are important for the adaptation to environmental stress conditions. Here we identified regulatory elements controlling the T6SS4 of Yersinia pseudotuberculosis and found a novel type of hexameric transcription factor, RovC. RovC directly interacts with the T6SS4 promoter region and activates T6SS4 transcription alone or in cooperation with the LysR-type regulator RovM. A higher complexity of regulation was achieved by the nutrient-responsive global regulator CsrA, which controls rovC expression on the transcriptional and post-transcriptional level. In summary, our work unveils a central mechanism in which RovC, a novel key activator, orchestrates the expression of the T6SS weapons together with a global regulator to deploy the system in response to the availability of nutrients in the species' native environment.
PubMed: 32966346
DOI: 10.1371/journal.ppat.1008552
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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