7W9H
Crystal structure of the receiver domain of the transcription regulator FleR from Pseudomonas aeruginosa
Summary for 7W9H
Entry DOI | 10.2210/pdb7w9h/pdb |
Descriptor | Response regulator protein FleR, CALCIUM ION, ACETATE ION, ... (4 entities in total) |
Functional Keywords | transcription |
Biological source | Pseudomonas aeruginosa PAO1 |
Total number of polymer chains | 2 |
Total formula weight | 28942.40 |
Authors | Sahoo, P.K.,Sheenu, n.,Jain, D. (deposition date: 2021-12-09, release date: 2022-12-14, Last modification date: 2024-01-03) |
Primary citation | Sahoo, P.K.,Jain, D. REC domain stabilizes the active heptamer of sigma 54 -dependent transcription factor, FleR from Pseudomonas aeruginosa. Iscience, 26:108397-108397, 2023 Cited by PubMed Abstract: Motility in is mediated through a single, polar flagellum, which is essential for virulence, colonization, and biofilm formation. FleSR, a two-component system (TCS), serves as a critical checkpoint in flagellar assembly. FleR is a σ-dependent response regulator that undergoes phosphorylation via cognate sensor kinase FleS for the assembly of the functionally active form. The active form remodels the σ-RNAP complex to initiate transcription. Small-angle X-ray scattering, crystallography, and negative staining electron microscopy reconstructions of FleR revealed that it exists predominantly as a dimer in the inactive form with low ATPase activity and assembles into heptamers upon phosphorylation with amplified ATPase activity. We establish that receiver (REC) domain stabilizes the heptamers and is indispensable for assembly of the functional phosphorylated form of FleR. The structural, biochemical, and complementation assays provide details of the phosphorylation-mediated assembly of FleR to regulate the expression of flagellar genes. PubMed: 38058307DOI: 10.1016/j.isci.2023.108397 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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