Team:Goettingen/Team/DAC

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===DAC Team===
===DAC Team===
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<p>Another approach of our project is the determination of the 3D structure of diadenylate cyclase (DAC) via crystallography and electron microscopy.</p>
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<p>Another approach of our project is the determination of the 3D structure of diadenylate cyclase (DAC) from the human pathogen <i>Listeria moncytogenes</i> by crystallography.</p>
<p>The advantage of the 3D structure of a protein received by crystallography is the identification of possible chemical binding sites due to computational modeling. These chemical compounds may interfere with the activity of the cyclase and could therefore be used as a potential starting point for further drug development.</p>
<p>The advantage of the 3D structure of a protein received by crystallography is the identification of possible chemical binding sites due to computational modeling. These chemical compounds may interfere with the activity of the cyclase and could therefore be used as a potential starting point for further drug development.</p>
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<p>Due to the fact that the diadenylate cyclase from Bacillus subtilis is difficult to crystallize, the full length protein from Listeria is going to be isolated and crystallized. Furthermore, Streptococcus and Staphylococcus will be used to obtain only the DAC domain of the protein for our analysis.</p>
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<p>Due to the fact that the diadenylate cyclase from Bacillus subtilis is difficult to crystallize, the full length protein from <i>Listeria</i> is going to be isolated and crystallized. Furthermore, <i>Streptococcus</i> and <i>Staphylococcus</i> will be used to obtain only the DAC domain of the protein for our analysis.</p>
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Revision as of 08:36, 27 September 2013





The beast and its Achilles heel:

 A novel target to fight multi-resistant pathogenic bacteria



DAC Team

Another approach of our project is the determination of the 3D structure of diadenylate cyclase (DAC) from the human pathogen Listeria moncytogenes by crystallography.

The advantage of the 3D structure of a protein received by crystallography is the identification of possible chemical binding sites due to computational modeling. These chemical compounds may interfere with the activity of the cyclase and could therefore be used as a potential starting point for further drug development.

Due to the fact that the diadenylate cyclase from Bacillus subtilis is difficult to crystallize, the full length protein from Listeria is going to be isolated and crystallized. Furthermore, Streptococcus and Staphylococcus will be used to obtain only the DAC domain of the protein for our analysis.

 

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