3IX4

LasR-TP1 complex

3IX4 の概要

• エントリーDOI: 10.2210/pdb3ix4/pdb
• 関連するPDBエントリー: 3IX3 3IX8
• 分子名称: Transcriptional activator protein lasR, 2,4-dibromo-6-({[(2-nitrophenyl)carbonyl]amino}methyl)phenyl 2-chlorobenzoate (3 entities in total)
• 機能のキーワード: quorum sensing, triphenyl mimic, activator, dna-binding, transcription, transcription regulation
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 159139.65

構造登録者

Zou, Y.,Nair, S.K. (登録日: 2009-09-03, 公開日: 2009-09-15, 最終更新日: 2023-09-06)

主引用文献

Zou, Y.,Nair, S.K.
Molecular basis for the recognition of structurally distinct autoinducer mimics by the Pseudomonas aeruginosa LasR quorum-sensing signaling receptor.
Chem.Biol., 16:961-970, 2009

PubMed Abstract: The human pathogen Pseudomonas aeruginosa coordinates the expression of virulence factors using quorum sensing, a signaling cascade triggered by the activation of signal receptors by small-molecule autoinducers. These homoserine lactone autoinducers stabilize their cognate receptors and activate their functions as transcription factors. Because quorum sensing regulates the progression of infection and host immune resistance, significant efforts have been devoted toward the identification of small molecules that disrupt this process. Screening efforts have identified a class of triphenyl compounds that are structurally distinct from the homoserine lactone autoinducer, yet interact specifically and potently with LasR receptor to modulate quorum sensing (Muh et al., 2006a). Here we present the high-resolution crystal structures of the ligand binding domain of LasR in complex with the autoinducer N-3-oxo-dodecanoyl homoserine lactone (1.4 A resolution), and with the triphenyl mimics TP-1, TP-3, and TP-4 (to between 1.8 A and 2.3 A resolution). These crystal structures provide a molecular rationale for understanding how chemically distinct compounds can be accommodated by a highly selective receptor, and provide the framework for the development of novel quorum-sensing regulators, utilizing the triphenyl scaffold.

PubMed: 19778724
DOI: 10.1016/j.chembiol.2009.09.001

実験手法

X-RAY DIFFRACTION (1.8 Å)