1l3l

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[[Image:1l3l.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3l OCA], [http://www.ebi.ac.uk/pdbsum/1l3l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l3l RCSB]</span>
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'''Crystal structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA'''
'''Crystal structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA'''
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[[Category: Winans, S C.]]
[[Category: Winans, S C.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
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[[Category: alpha/beta/alpha sandwich]]
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[[Category: Alpha/beta/alpha sandwich]]
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[[Category: asymmetry of the protein-dna complex]]
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[[Category: Asymmetry of the protein-dna complex]]
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[[Category: helix-turn-helix dna binding motif]]
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Revision as of 20:30, 2 May 2008

Template:STRUCTURE 1l3l

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


Overview

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.

About this Structure

1L3L is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA., Zhang RG, Pappas T, Brace JL, Miller PC, Oulmassov T, Molyneaux JM, Anderson JC, Bashkin JK, Winans SC, Joachimiak A, Nature. 2002 Jun 27;417(6892):971-4. PMID:12087407 Page seeded by OCA on Fri May 2 23:30:10 2008

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