7EJW
Crystal structure of FleN in complex with FleQ AAA+ doamain
Summary for 7EJW
Entry DOI | 10.2210/pdb7ejw/pdb |
Descriptor | Transcriptional antiactivator FleN, Transcriptional regulator FleQ, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (6 entities in total) |
Functional Keywords | antiactivator, activator, atpase, transcription, fleq, flen |
Biological source | Pseudomonas aeruginosa PAO1 More |
Total number of polymer chains | 4 |
Total formula weight | 120401.41 |
Authors | Chanchal,Banerjee, P.,Raghav, S.,Jain, D. (deposition date: 2021-04-02, release date: 2021-12-22, Last modification date: 2024-05-29) |
Primary citation | Banerjee, P.,Raghav, S.,Goswami, H.N.,Jain, D. The antiactivator FleN uses an allosteric mechanism to regulate sigma 54 -dependent expression of flagellar genes in Pseudomonas aeruginosa . Sci Adv, 7:eabj1792-eabj1792, 2021 Cited by PubMed Abstract: Diverse sigma factors associate with the RNA polymerase (RNAP) core enzyme to initiate transcription of specific target genes in bacteria. σ-Mediated transcription uses AAA+ activators that utilize their ATPase activity for transcription initiation. FleQ is a σ-dependent master transcriptional regulator of flagellar genes in . The ATPase activity of FleQ is regulated via a P-loop ATPase, FleN, through protein-protein interaction. We report a high-resolution crystal structure of the AAA+ domain of FleQ in complex with antiactivator FleN. The data reveal that FleN allosterically prevents ATP binding to FleQ. Furthermore, FleN remodels the region of FleQ essential for engagement with σ for transcription initiation. Disruption of the conserved protein-protein interface, by mutation, shows motility and transcription defects in vivo and multiflagellate phenotype. Our study provides a detailed mechanism used by monoflagellate bacteria to fine-tune the expression of flagellar genes to form and maintain a single flagellum. PubMed: 34669473DOI: 10.1126/sciadv.abj1792 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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