5LEK

The Transcriptional Regulator PrfA-G145S mutant from Listeria Monocytogenes in complex with a 30-bp operator PrfA-box motif

5LEK の概要

• エントリーDOI: 10.2210/pdb5lek/pdb
• 関連するPDBエントリー: 2beo
• 分子名称: Listeriolysin regulatory protein, DNA (30-MER), ... (4 entities in total)
• 機能のキーワード: transcription regulator, dna binding, activation, listeria monocytogenes, transcription
• 由来する生物種: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 73160.79

構造登録者

Hall, M.,Grundstrom, C.,Begum, A.,Lindberg, M.,Sauer, U.H.,Almqvist, F.,Johansson, J.,Sauer-Eriksson, A.E. (登録日: 2016-06-29, 公開日: 2016-12-07, 最終更新日: 2024-01-10)

主引用文献

Hall, M.,Grundstrom, C.,Begum, A.,Lindberg, M.J.,Sauer, U.H.,Almqvist, F.,Johansson, J.,Sauer-Eriksson, A.E.
Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.
Proc. Natl. Acad. Sci. U.S.A., 113:14733-14738, 2016

PubMed Abstract: Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfA in complex only with DNA confirms that PrfA can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction.

PubMed: 27930316
DOI: 10.1073/pnas.1614028114

実験手法

X-RAY DIFFRACTION (2.8 Å)