1L3L

Crystal structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA

1L3L の概要

• エントリーDOI: 10.2210/pdb1l3l/pdb
• 分子名称: 5'-D(*GP*AP*TP*GP*TP*GP*CP*AP*GP*AP*TP*CP*TP*GP*CP*AP*CP*AP*TP*C)-3', Transcriptional activator protein traR, 3-OXO-OCTANOIC ACID (2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE, ... (4 entities in total)
• 機能のキーワード: helix-turn-helix dna binding motif, alpha/beta/alpha sandwich, asymmetry of the protein-dna complex, transcription-dna complex, transcription/dna
• 由来する生物種: Agrobacterium tumefaciens
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 133741.20

構造登録者

Zhang, R.,Pappas, T.,Brace, J.L.,Miller, P.C.,Oulmassov, T.,Molyneaux, J.M.,Anderson, J.C.,Bashkin, J.K.,Winans, S.C.,Joachimiak, A. (登録日: 2002-02-27, 公開日: 2002-07-03, 最終更新日: 2024-10-09)

主引用文献

Zhang, R.G.,Pappas, T.,Brace, J.L.,Miller, P.C.,Oulmassov, T.,Molyneaux, J.M.,Anderson, J.C.,Bashkin, J.K.,Winans, S.C.,Joachimiak, A.
Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA.
Nature, 417:971-974, 2002

PubMed Abstract: Many proteobacteria are able to monitor their population densities through the release of pheromones known as N-acylhomoserine lactones. At high population densities, these pheromones elicit diverse responses that include bioluminescence, biofilm formation, production of antimicrobials, DNA exchange, pathogenesis and symbiosis. Many of these regulatory systems require a pheromone-dependent transcription factor similar to the LuxR protein of Vibrio fischeri. Here we present the structure of a LuxR-type protein. TraR of Agrobacterium tumefaciens was solved at 1.66 A as a complex with the pheromone N-3-oxooctanoyl-L-homoserine lactone (OOHL) and its TraR DNA-binding site. The amino-terminal domain of TraR is an alpha/beta/alpha sandwich that binds OOHL, whereas the carboxy-terminal domain contains a helix turn helix DNA-binding motif. The TraR dimer displays a two-fold symmetry axis in each domain; however, these two axes of symmetry are at an approximately 90 degree angle, resulting in a pronounced overall asymmetry of the complex. The pheromone lies fully embedded within the protein with virtually no solvent contact, and makes numerous hydrophobic contacts with the protein as well as four hydrogen bonds: three direct and one water-mediated.

PubMed: 12087407
DOI: 10.1038/nature00833

実験手法

X-RAY DIFFRACTION (1.66 Å)