Difference between revisions of "Part:BBa K1045003"

Line 5: Line 5:
 
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 harmful to 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 [[Part:BBa_K1045003|BBa_K1045003]] described here, covers the amino acids 100 to 273 of the full length coding sequence of CdaA. <br /> For a precise description of this part, please vistit the experience page!
 
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 harmful to 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 [[Part:BBa_K1045003|BBa_K1045003]] described here, covers the amino acids 100 to 273 of the full length coding sequence of CdaA. <br /> For a precise description of this part, please vistit the experience page!
 
<p>
 
<p>
<html><object width="420" height="315"><param name="movie" value="http://youtu.be/T0xpaOZtjfk;version=3&amp;rel=0"></param><param name="allowFullScreen" value="true"></param><param name="allowscriptaccess" value="always"></param><embed src="http://youtu.be/T0xpaOZtjfk;rel=0" type="application/x-shockwave-flash" width="420" height="315" allowscriptaccess="always" allowfullscreen="true"></embed></object></html>
+
<embed
 +
width="420" height="345"
 +
src="http://youtu.be/T0xpaOZtjfk"
 +
type="application/x-shockwave-flash">
 +
</embed>
 
</p>
 
</p>
 
http://youtu.be/T0xpaOZtjfk
 
http://youtu.be/T0xpaOZtjfk

Revision as of 16:41, 28 October 2013

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 harmful to 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.
For a precise description of this part, please vistit the experience page!

<embed width="420" height="345" src="http://youtu.be/T0xpaOZtjfk" type="application/x-shockwave-flash"> </embed>

http://youtu.be/T0xpaOZtjfk


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]