7T8I

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

7T8I の概要

• エントリーDOI: 10.2210/pdb7t8i/pdb
• 分子名称: Phage element (ICEBs1)transcriptional regulator (Xre family) (3 entities in total)
• 機能のキーワード: hth-dna binding domain, dimerisation, immunity repressor protein, bacterial infection, horizontal gene transfer, dna binding protein
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14997.74

構造登録者

Caliandro, R.,de Diego, I.,Gomis-Ruth, F.X. (登録日: 2021-12-16, 公開日: 2022-03-16, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)