8DQ0
Quorum-sensing receptor RhlR bound to PqsE
Summary for 8DQ0
| Entry DOI | 10.2210/pdb8dq0/pdb |
| EMDB information | 27645 |
| Descriptor | RhlR protein, 2-aminobenzoylacetyl-CoA thioesterase, 4-(3-bromophenoxy)-N-[(3S)-2-oxothiolan-3-yl]butanamide (3 entities in total) |
| Functional Keywords | transcriptional regulators, quorum sensing, dna binding, transcription |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 4 |
| Total formula weight | 124640.29 |
| Authors | Paczkowski, J.E.,Fromme, J.C.,Feathers, J.R. (deposition date: 2022-07-18, release date: 2022-12-07, Last modification date: 2025-05-14) |
| Primary citation | Feathers, J.R.,Richael, E.K.,Simanek, K.A.,Fromme, J.C.,Paczkowski, J.E. Structure of the RhlR-PqsE complex from Pseudomonas aeruginosa reveals mechanistic insights into quorum-sensing gene regulation. Structure, 30:1626-, 2022 Cited by PubMed Abstract: Pseudomonas aeruginosa is an opportunistic pathogen that is responsible for thousands of deaths every year in the United States. P. aeruginosa virulence factor production is mediated by quorum sensing, a mechanism of bacterial cell-cell communication that relies on the production and detection of signal molecules called autoinducers. In P. aeruginosa, the transcription factor receptor RhlR is activated by a RhlI-synthesized autoinducer. We recently showed that RhlR-dependent transcription is enhanced by a physical interaction with the enzyme PqsE via increased affinity of RhlR for promoter DNA. However, the molecular basis for complex formation and how complex formation enhanced RhlR transcriptional activity remained unclear. Here, we report the structure of ligand-bound RhlR in complex with PqsE. Additionally, we determined the structure of the complex bound with DNA, revealing the mechanism by which RhlR-mediated transcription is enhanced by PqsE, thereby establishing the molecular basis for RhlR-dependent virulence factor production in P. aeruginosa. PubMed: 36379213DOI: 10.1016/j.str.2022.10.008 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.74 Å) |
Structure validation
Download full validation report
