Team:Goettingen/Team/DAC

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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>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>
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<p>Once having a 3D structure of a protein in hand potential inhibitor binding sites can be identified by 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>Once having a 3D structure of a protein in hand potential inhibitor binding sites can be identified by computational modeling. Promising inhibitors that interfere with DAC activity could be used as a starting point for the development of drugs with improved inhibitory efficiency.</p>
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<p>Due to the fact that the diadenylate cyclase from <i>Bacillus subtilis</i> 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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<p>Due to the fact that the DAC from <i>Bacillus subtilis</i> is difficult to purify and thus to crystallize, we have decided to crystallize the DAC protein from <i>Listeria</i> . In addition to this, we will try to crystallize the DACs from <i>Streptococcus</i> and <i>Staphylococcus</i> .</p>
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Revision as of 08:45, 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.

Once having a 3D structure of a protein in hand potential inhibitor binding sites can be identified by computational modeling. Promising inhibitors that interfere with DAC activity could be used as a starting point for the development of drugs with improved inhibitory efficiency.

Due to the fact that the DAC from Bacillus subtilis is difficult to purify and thus to crystallize, we have decided to crystallize the DAC protein from Listeria . In addition to this, we will try to crystallize the DACs from Streptococcus and Staphylococcus .

 

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