Part:BBa_K1045003
Diadenylate cyclase domain of Listeria monocytogenes cdaA (DacA)
The severe threat 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.
Cyclic di-AMP was discovered to be an essential signal molecule in Gram-positive bacteria including the pathogenic species Streptococcus pneumoniae, Staphylococcus aureus and Listeria 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 two 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 as well as humans. Here, we introduce a truncated but functional DAC which localizes to the cytosol and can easily be purified. Furthermore, protein crystals were obtained as well as 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.
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Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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