5HS8

Crystal structure of the diamide-treated YodB from B. subtilis

5HS8 の概要

• エントリーDOI: 10.2210/pdb5hs8/pdb
• 関連するPDBエントリー: 5HS7 5HS9
• 分子名称: HTH-type transcriptional regulator YodB (2 entities in total)
• 機能のキーワード: hth-type transcriptional regulator, oxidized form, dna binding protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12725.84

構造登録者

Lee, S.J.,Lee, I.G.,Lee, B.J. (登録日: 2016-01-25, 公開日: 2016-08-17, 最終更新日: 2024-11-13)

主引用文献

Lee, S.J.,Lee, I.G.,Lee, K.Y.,Kim, D.G.,Eun, H.J.,Yoon, H.J.,Chae, S.,Song, S.H.,Kang, S.O.,Seo, M.D.,Kim, H.S.,Park, S.J.,Lee, B.J.
Two distinct mechanisms of transcriptional regulation by the redox sensor YodB
Proc.Natl.Acad.Sci.USA, 113:E5202-E5211, 2016

PubMed Abstract: For bacteria, cysteine thiol groups in proteins are commonly used as thiol-based switches for redox sensing to activate specific detoxification pathways and restore the redox balance. Among the known thiol-based regulatory systems, the MarR/DUF24 family regulators have been reported to sense and respond to reactive electrophilic species, including diamide, quinones, and aldehydes, with high specificity. Here, we report that the prototypical regulator YodB of the MarR/DUF24 family from Bacillus subtilis uses two distinct pathways to regulate transcription in response to two reactive electrophilic species (diamide or methyl-p-benzoquinone), as revealed by X-ray crystallography, NMR spectroscopy, and biochemical experiments. Diamide induces structural changes in the YodB dimer by promoting the formation of disulfide bonds, whereas methyl-p-benzoquinone allows the YodB dimer to be dissociated from DNA, with little effect on the YodB dimer. The results indicate that B. subtilis may discriminate toxic quinones, such as methyl-p-benzoquinone, from diamide to efficiently manage multiple oxidative signals. These results also provide evidence that different thiol-reactive compounds induce dissimilar conformational changes in the regulator to trigger the separate regulation of target DNA. This specific control of YodB is dependent upon the type of thiol-reactive compound present, is linked to its direct transcriptional activity, and is important for the survival of B. subtilis This study of B. subtilis YodB also provides a structural basis for the relationship that exists between the ligand-induced conformational changes adopted by the protein and its functional switch.

PubMed: 27531959
DOI: 10.1073/pnas.1604427113

実験手法

X-RAY DIFFRACTION (2 Å)