Anthrax edema factor

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Contents

Function

Anthrax edema factor (EF) or calmodulin-sensitive adenylate cyclase is an enzyme which is part of the Bacillus anthracis anthrax toxin. The full anthrax toxin is composed of -

The EF is a calcium- and calmodulin-dependent adenylate cyclase. The binding of calmodulin to EF changes it from its non-active form to the active one.[1] See also Toxins.

Disease

The anthrax disease is caused by the invasion of cells by the bacteria followed by increasing the cellular level of cAMP thus upsetting water homeostasis and causing disruption of signaling pathways.

Structural highlights

  • EF trimer with 3 calmodulin molecules.
  • ADP derivative/Yt+3 binding site of EF. Water molecules are shown as red spheres.
  • Ca+2 binding site of calmodulin (PDB code 1pk0).[2]

3D structures of anthrax edema factor

Anthrax edema factor 3D structures


EF trimer (magenta, cyan, salmon) complex with calmodulin (yellow) and adenine diphosphate derivative, Ca+2 (light green) and Yt+3 (green) ions (PDB code 1pk0).

Drag the structure with the mouse to rotate


References

  1. Abrami L, Reig N, van der Goot FG. Anthrax toxin: the long and winding road that leads to the kill. Trends Microbiol. 2005 Feb;13(2):72-8. PMID:15680766 doi:http://dx.doi.org/10.1016/j.tim.2004.12.004
  2. Shen Y, Zhukovskaya NL, Zimmer MI, Soelaiman S, Bergson P, Wang CR, Gibbs CS, Tang WJ. Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3242-7. Epub 2004 Feb 20. PMID:14978283 doi:10.1073/pnas.0306552101

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Michal Harel, Alexander Berchansky

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