Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractVOC transport in an occupied residence: Measurements and predictions via deep learning    Next AbstractOxidative damage and antioxidant responses in Microcystis aeruginosa exposed to the allelochemical berberine isolated from golden thread »

Nature


Title:Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA
Author(s):Zhang RG; Pappas KM; Brace JL; Miller PC; Oulmassov T; Molyneaux JM; Anderson JC; Bashkin JK; Winans SC; Joachimiak A;
Address:"Bioscience Division/Structural Biology Center, Argonne National Laboratory, 9700 S. Cass Avenue, Argonne, Illinois 60439, USA"
Journal Title:Nature
Year:2002
Volume:417
Issue:6892
Page Number:971 - 974
DOI: 10.1038/nature00833
ISSN/ISBN:0028-0836 (Print) 0028-0836 (Linking)
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"
Keywords:"Amino Acid Sequence Bacterial Proteins/*chemistry/*metabolism Binding Sites Crystallography, X-Ray DNA, Bacterial/genetics/*metabolism DNA-Binding Proteins/chemistry/metabolism Dimerization Helix-Turn-Helix Motifs Homoserine/*analogs & derivatives/metabol;"
Notes:"MedlineZhang, Rong-guang Pappas, Katherine M Brace, Jennifer L Miller, Paula C Oulmassov, Tim Molyneaux, John M Anderson, John C Bashkin, James K Winans, Stephen C Joachimiak, Andrzej eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. England 2002/06/28 Nature. 2002 Jun 27; 417(6892):971-4. doi: 10.1038/nature00833"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 24-12-2024