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

被引:345
作者
Zhang, RG
Pappas, T
Brace, JL
Miller, PC
Oulmassov, T
Molyneauz, JM
Anderson, JC
Bashkin, JK
Winans, SC
Joachimiak, A
机构
[1] Argonne Natl Lab, Biosci Div, Struct Biol Ctr, Argonne, IL 60439 USA
[2] Cornell Univ, Dept Microbiol, Ithaca, NY 14853 USA
[3] Monsanto Co, St Louis, MO 63167 USA
关键词
D O I
10.1038/nature00833
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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(1). 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 Angstrom 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 90degrees 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.
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页码:971 / 974
页数:4
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