Difference between revisions of "Part:BBa K1045003"

Revision as of 13:30, 25 September 2013

Diadenylate cyclase domain of Listeria monocytogenes cdaA (DacA)

The severe thread caused by bacteria which are resistant to conventional antibiotic drugs and the appearance of even multi-resistant strains demonstrates the urgent need for the discovery of new antibacterial substance classes. c-di-AMP was discovered to be an essential signal molecule in Gram-positive bacteria including the pathogenic species S. Pneumoniae, S. aureus, and L. monocytogenes. Both loss and overproduction of c-di-AMP have detrimental effects on cell growth, cell wall synthesis, and propagation. Thus, the diadenylate cyclase (DAC) which catalyses the condensation reaction of 2 ATP molecules to c-di-AMP is the key factor for signal molecule production and maintenance of c-di-AMP homeostasis. We are convinced that the DAC is a very promising target for the development of highly specific antibiotic substances which exclusively act on Gram-positive bacteria and are not harming Gram-negative ones, including the gut bacterium Escherichia coli. Here, we introduce a truncated but functional DAC which localizes to the cytosol and can easily be purified. Furthermore, protein crystals were obtained enabling the determination the of the protein structure by X-ray diffraction analysis. The part BBa_K1045003 described here, covers the amino acids 100 to 273 of the full length coding sequence of CdaA.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K1045003 short</partinfo>
-Cyclic di-AMP is involved in cell signaling of Gram positive bacteria including ''L. monocytogenes'', ''B. subtilis'', ''S. aureus'', and ''S. pneumoniae''.
+The severe thread caused by bacteria which are resistant to conventional antibiotic drugs and the appearance of even multi-resistant strains demonstrates the urgent need for the discovery of new antibacterial substance classes.
-The diadenylate cyclase domain of ''Listeria monocytogenes'' CdaA protein generates cyclic di-AMP for cell signaling. The part [[Part:BBa_K1045003|BBa_K1045003]] described here, covers the amino acids 100 to 273 of the full length coding sequence of CdaA.
+c-di-AMP was discovered to be an essential signal molecule in Gram-positive bacteria including the pathogenic species S. Pneumoniae, S. aureus, and L. monocytogenes. Both loss and overproduction of c-di-AMP have detrimental effects on cell growth, cell wall synthesis, and propagation. Thus, the diadenylate cyclase (DAC) which catalyses the condensation reaction of 2 ATP molecules to c-di-AMP is the key factor for signal molecule production and maintenance of c-di-AMP homeostasis. We are convinced that the DAC is a very promising target for the development of highly specific antibiotic substances which exclusively act on Gram-positive bacteria and are not harming Gram-negative ones, including the gut bacterium Escherichia coli. Here, we introduce a truncated but functional DAC which localizes to the cytosol and can easily be purified. Furthermore, protein crystals were obtained enabling the determination the of the protein structure by X-ray diffraction analysis. The part [[Part:BBa_K1045003|BBa_K1045003]] described here, covers the amino acids 100 to 273 of the full length coding sequence of CdaA.
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