7X9S
Crystal structure of a complex between the antirepressor GmaR and the transcriptional repressor MogR
Summary for 7X9S
| Entry DOI | 10.2210/pdb7x9s/pdb |
| Descriptor | GmaR, Motility gene repressor MogR (2 entities in total) |
| Functional Keywords | antirepressor, repressor, transferase, protein binding-transcription complex, protein binding, protein binding/transcription |
| Biological source | Listeria monocytogenes More |
| Total number of polymer chains | 6 |
| Total formula weight | 201357.75 |
| Authors | Cho, S.Y.,Na, H.W.,Oh, H.B.,Kwak, Y.M.,Song, W.S.,Park, S.C.,Yoon, S.I. (deposition date: 2022-03-16, release date: 2022-11-23, Last modification date: 2023-11-29) |
| Primary citation | 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 Cited by 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: 36283692DOI: 10.1093/nar/gkac815 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.11 Å) |
Structure validation
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