7X9S

Crystal structure of a complex between the antirepressor GmaR and the transcriptional repressor MogR

7X9S の概要

• エントリーDOI: 10.2210/pdb7x9s/pdb
• 分子名称: GmaR, Motility gene repressor MogR (2 entities in total)
• 機能のキーワード: antirepressor, repressor, transferase, protein binding-transcription complex, protein binding, protein binding/transcription
• 由来する生物種: Listeria monocytogenes; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 201357.75

構造登録者

Cho, S.Y.,Na, H.W.,Oh, H.B.,Kwak, Y.M.,Song, W.S.,Park, S.C.,Yoon, S.I. (登録日: 2022-03-16, 公開日: 2022-11-23, 最終更新日: 2023-11-29)

主引用文献

Cho, S.Y.,Na, H.W.,Oh, H.B.,Kwak, Y.M.,Song, W.S.,Park, S.C.,Jeon, W.J.,Cho, H.,Oh, B.C.,Park, J.,Kang, S.G.,Lee, G.S.,Yoon, S.I.
Structural basis of flagellar motility regulation by the MogR repressor and the GmaR antirepressor in Listeria monocytogenes.
Nucleic Acids Res., 50:11315-11330, 2022

PubMed Abstract: The pathogenic Listeria monocytogenes bacterium produces the flagellum as a locomotive organelle at or below 30°C outside the host, but it halts flagellar expression at 37°C inside the human host to evade the flagellum-induced immune response. Listeria monocytogenes GmaR is a thermosensor protein that coordinates flagellar expression by binding the master transcriptional repressor of flagellar genes (MogR) in a temperature-responsive manner. To understand the regulatory mechanism whereby GmaR exerts the antirepression activity on flagellar expression, we performed structural and mutational analyses of the GmaR-MogR system. At or below 30°C, GmaR exists as a functional monomer and forms a circularly enclosed multidomain structure via an interdomain interaction. GmaR in this conformation recognizes MogR using the C-terminal antirepressor domain in a unique dual binding mode and mediates the antirepressor function through direct competition and spatial restraint mechanisms. Surprisingly, at 37°C, GmaR rapidly forms autologous aggregates that are deficient in MogR neutralization capabilities.

PubMed: 36283692
DOI: 10.1093/nar/gkac815

実験手法

X-RAY DIFFRACTION (3.11 Å)