1l3l
From Proteopedia
(New page: 200px<br /><applet load="1l3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3l, resolution 1.66Å" /> '''Crystal structure of...) |
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| - | [[Image:1l3l.gif|left|200px]]<br /><applet load="1l3l" size=" | + | [[Image:1l3l.gif|left|200px]]<br /><applet load="1l3l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l3l, resolution 1.66Å" /> | caption="1l3l, resolution 1.66Å" /> | ||
'''Crystal structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA'''<br /> | '''Crystal structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many proteobacteria are able to monitor their population densities through | + | 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== | ==About this Structure== | ||
| - | 1L3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with LAE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1L3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with <scene name='pdbligand=LAE:'>LAE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Agrobacterium tumefaciens]] | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, J | + | [[Category: Anderson, J C.]] |
| - | [[Category: Bashkin, J | + | [[Category: Bashkin, J K.]] |
| - | [[Category: Brace, J | + | [[Category: Brace, J L.]] |
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
| - | [[Category: Miller, P | + | [[Category: Miller, P C.]] |
| - | [[Category: Molyneaux, J | + | [[Category: Molyneaux, J M.]] |
[[Category: Oulmassov, T.]] | [[Category: Oulmassov, T.]] | ||
[[Category: Pappas, T.]] | [[Category: Pappas, T.]] | ||
| - | [[Category: Winans, S | + | [[Category: Winans, S C.]] |
[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
[[Category: LAE]] | [[Category: LAE]] | ||
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[[Category: helix-turn-helix dna binding motif]] | [[Category: helix-turn-helix dna binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:56 2008'' |
Revision as of 11:40, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 13:40:56 2008
Categories: Agrobacterium tumefaciens | Single protein | Anderson, J C. | Bashkin, J K. | Brace, J L. | Joachimiak, A. | Miller, P C. | Molyneaux, J M. | Oulmassov, T. | Pappas, T. | Winans, S C. | Zhang, R. | LAE | Alpha/beta/alpha sandwich | Asymmetry of the protein-dna complex | Helix-turn-helix dna binding motif
