8DQ0

Quorum-sensing receptor RhlR bound to PqsE

8DQ0 の概要

• エントリーDOI: 10.2210/pdb8dq0/pdb
• EMDBエントリー: 27645
• 分子名称: RhlR protein, 2-aminobenzoylacetyl-CoA thioesterase, 4-(3-bromophenoxy)-N-[(3S)-2-oxothiolan-3-yl]butanamide (3 entities in total)
• 機能のキーワード: transcriptional regulators, quorum sensing, dna binding, transcription
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 124640.29

構造登録者

Paczkowski, J.E.,Fromme, J.C.,Feathers, J.R. (登録日: 2022-07-18, 公開日: 2022-12-07, 最終更新日: 2025-05-14)

主引用文献

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

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: 36379213
DOI: 10.1016/j.str.2022.10.008

実験手法

ELECTRON MICROSCOPY (3.74 Å)