7T8I

Crystal structure of the ImmR transcriptional regulator DNA-binding domain of Bacillus subtilis

Summary for 7T8I

• Entry DOI: 10.2210/pdb7t8i/pdb
• Descriptor: Phage element (ICEBs1)transcriptional regulator (Xre family) (3 entities in total)
• Functional Keywords: hth-dna binding domain, dimerisation, immunity repressor protein, bacterial infection, horizontal gene transfer, dna binding protein
• Biological source: Bacillus subtilis; More
• Total number of polymer chains: 2
• Total formula weight: 14997.74

Authors

Caliandro, R.,de Diego, I.,Gomis-Ruth, F.X. (deposition date: 2021-12-16, release date: 2022-03-16, Last modification date: 2024-04-03)

Primary citation

Caliandro, R.,de Diego, I.,Gomis-Ruth, F.X.
Crystal structure report of the ImmR transcriptional regulator DNA-binding domain of the Bacillus subtilis ICEBs1 transposon.
Sci Rep, 12:5258-5258, 2022

PubMed Abstract: Bacillus subtilis is a commensal member of the human oral and gut microbiomes, which can become infectious to immunocompromised patients. It possesses a conjugative transposon, ICEBs1, which includes > 20 genes and can be passed by horizontal gene transfer to other bacteria, including pathogenic Bacillus anthracis and Listeria monocytogenes. ICEBs1 is regulated by the ImmR/ImmA tandem, which are a transcriptional repressor that constitutively blocks transcription and a metallopeptidase that acts as anti-repressor and inactivates ImmR by proteolytic cleavage. We here report the production and purification of 127-residue ImmR from ICEBs1 and the crystal structure of its DNA-binding domain. It features a five-helix bundle centred on a helix-turn-helix motif potentially binding the major grove of double-stranded target DNA. ImmR shows structural and mechanistic similarity with the B. subtilis SinR repressor, which is engaged in sporulation inhibition.

PubMed: 35347179
DOI: 10.1038/s41598-022-09237-2

Experimental method

X-RAY DIFFRACTION (2.1 Å)