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==Overview==
==Overview==
The quorum sensing system allows bacteria to sense their cell density and, initiate an altered pattern of gene expression after a sufficient quorum, of cells has accumulated. In Agrobacterium tumefaciens, quorum sensing, controls conjugal transfer of the tumour- inducing plasmid, responsible, for plant crown gall disease. The core components of this system are the, transcriptional regulator TraR and its inducing ligand, N-(3-oxo-octanoyl)-L-homoserine lactone. This complex binds DNA and, activates gene expression. We have determined the crystal structure of, TraR in complex with its autoinducer and target DNA (PDB code 1h0m). The, protein is dimeric, with each monomer composed of an N-terminal domain, which binds the ligand in an enclosed cavity far from the dimerization, region, and a C-terminal domain, which binds DNA via a helix-turn-helix, motif. The structure reveals an asymmetric homodimer, with one monomer, longer than the other. The N-terminal domain resembles GAF/PAS domains, normally fused to catalytic signalling domains. In TraR, the gene fusion, is between a GAF/PAS domain and a DNA-binding domain, resulting in a, specific transcriptional regulator involved in quorum sensing.
The quorum sensing system allows bacteria to sense their cell density and initiate an altered pattern of gene expression after a sufficient quorum of cells has accumulated. In Agrobacterium tumefaciens, quorum sensing controls conjugal transfer of the tumour- inducing plasmid, responsible for plant crown gall disease. The core components of this system are the transcriptional regulator TraR and its inducing ligand N-(3-oxo-octanoyl)-L-homoserine lactone. This complex binds DNA and activates gene expression. We have determined the crystal structure of TraR in complex with its autoinducer and target DNA (PDB code 1h0m). The protein is dimeric, with each monomer composed of an N-terminal domain, which binds the ligand in an enclosed cavity far from the dimerization region, and a C-terminal domain, which binds DNA via a helix-turn-helix motif. The structure reveals an asymmetric homodimer, with one monomer longer than the other. The N-terminal domain resembles GAF/PAS domains, normally fused to catalytic signalling domains. In TraR, the gene fusion is between a GAF/PAS domain and a DNA-binding domain, resulting in a specific transcriptional regulator involved in quorum sensing.


==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Cortese, R.]]
[[Category: Cortese, R.]]
[[Category: Francesco, R.De.]]
[[Category: Francesco, R De.]]
[[Category: Gargioli, C.]]
[[Category: Gargioli, C.]]
[[Category: Marco, S.Di.]]
[[Category: Marco, S Di.]]
[[Category: Muraglia, E.]]
[[Category: Muraglia, E.]]
[[Category: Neddermann, P.]]
[[Category: Neddermann, P.]]
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[[Category: trar]]
[[Category: trar]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:44:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:08 2008''

Revision as of 13:56, 21 February 2008

File:1h0m.gif


1h0m, resolution 3.00Å

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THREE-DIMENSIONAL STRUCTURE OF THE QUORUM SENSING PROTEIN TRAR BOUND TO ITS AUTOINDUCER AND TO ITS TARGET DNA

OverviewOverview

The quorum sensing system allows bacteria to sense their cell density and initiate an altered pattern of gene expression after a sufficient quorum of cells has accumulated. In Agrobacterium tumefaciens, quorum sensing controls conjugal transfer of the tumour- inducing plasmid, responsible for plant crown gall disease. The core components of this system are the transcriptional regulator TraR and its inducing ligand N-(3-oxo-octanoyl)-L-homoserine lactone. This complex binds DNA and activates gene expression. We have determined the crystal structure of TraR in complex with its autoinducer and target DNA (PDB code 1h0m). The protein is dimeric, with each monomer composed of an N-terminal domain, which binds the ligand in an enclosed cavity far from the dimerization region, and a C-terminal domain, which binds DNA via a helix-turn-helix motif. The structure reveals an asymmetric homodimer, with one monomer longer than the other. The N-terminal domain resembles GAF/PAS domains, normally fused to catalytic signalling domains. In TraR, the gene fusion is between a GAF/PAS domain and a DNA-binding domain, resulting in a specific transcriptional regulator involved in quorum sensing.

About this StructureAbout this Structure

1H0M is a Protein complex structure of sequences from Agrobacterium tumefaciens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA., Vannini A, Volpari C, Gargioli C, Muraglia E, Cortese R, De Francesco R, Neddermann P, Marco SD, EMBO J. 2002 Sep 2;21(17):4393-401. PMID:12198141

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