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Title | Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 52, Issue 12, Page 7305-7320, Year 2024 |
Publish date | Jul 8, 2024 |
Authors | Markéta Šoltysová / Jana Škerlová / Petr Pachl / Karel Škubník / Milan Fábry / Irena Sieglová / Martina Farolfi / Irina Grishkovskaya / Michal Babiak / Jiří Nováček / Libor Krásný / Pavlína Řezáčová / |
PubMed Abstract | The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography ...The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics. |
External links | Nucleic Acids Res / PubMed:38842936 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.7 - 4.4 Å |
Structure data | EMDB-18864, PDB-8r3g: PDB-8r7y: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | DNA BINDING PROTEIN / Bacillus subtilis / transcription repressor / glucose catabolism / SorC family / transcriptional repressor / protein-DNA complex |