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

Rong-guang Zhang, Katherine M. Pappas, Jennifer L. Brace, Paula C. Miller, Tim Oulmassov, John M. Molyneaux, John C. Anderson, James K. Bashkin, Stephen C. Winans and Andrzej Joachimiak ()
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Rong-guang Zhang: Argonne National Laboratory
Katherine M. Pappas: Cornell University
Jennifer L. Brace: Argonne National Laboratory
Paula C. Miller: Monsanto Company
Tim Oulmassov: Monsanto Company
John M. Molyneaux: Monsanto Company
John C. Anderson: Monsanto Company
James K. Bashkin: Monsanto Company
Stephen C. Winans: Cornell University
Andrzej Joachimiak: Argonne National Laboratory

Nature, 2002, vol. 417, issue 6892, 971-974

Abstract: 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 symbiosis1. 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 Å 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 α/β/α 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° 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.

Date: 2002
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DOI: 10.1038/nature00833

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