Anthrax edema factor: Difference between revisions

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{{STRUCTURE_1xfw|  PDB=1xfw  | SIZE=400| SCENE= |right|CAPTION=EF complex with calmodulin and cAMP, Ca+2 and Mg+2 ions [[1xfw]] }}
<StructureSection load='1pk0' size='350' side='right' caption='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]]).' scene='48/485623/Cv/1'>
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'''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 -<BR />
-->
*A cell-binding protein [[Anthrax protective antigen]]<BR />
'''Anthrax edema factor''' (EF) is an enzyme which is part of the ''Bacillus anthracis'' anthrax toxin.  The anthrax toxin is composed of a cell-binding protein (protective antigen), lethal factor and EF.   The EF is a calcium- and calmodulin-dependent adenylate cyclase.  It causes the cellular level of cAMP to increase thus upsetting water homeostasis and causing disruption of signaling pathways.  
*[[Anthrax Lethal Factor]]<BR />
*and anthrax edema factor.<br />
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.<ref>PMID:15680766</ref> 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 ==
 
*<scene name='48/485623/Cv/2'>EF trimer with 3 calmodulin molecules</scene>.
*<scene name='48/485623/Cv/5'>ADP derivative/Yt+3 binding site</scene> of EF. Water molecules are shown as red spheres.
*<scene name='48/485623/Cv/6'>Ca+2 binding site</scene> of calmodulin (PDB code [[1pk0]]).<ref>PMID:14978283</ref>


==3D structures of anthrax edema factor==
==3D structures of anthrax edema factor==
[[Anthrax edema factor 3D structures]]
</StructureSection>


[[1lvc]] – EF adenylate cyclase domain + calmodulin + anthraniloyl-deoxy-ATP<br />
[[1pk0]] - EF adenylate cyclase domain + calmodulin + phosphonylmethoxyethyl-ADP<br />
[[1s26]] - EF adenylate cyclase domain + calmodulin + methylene-ATP<br />
[[1sk6]] - EF adenylate cyclase domain + calmodulin + pyrophosphate + cAMP<br />
[[1xfu]] - EF residues 64-800 (mutant) + calmodulin<br />
[[1xfv]] - EF residues 33-800 + calmodulin + deoxy-ATP<br />
[[1xfw]] - EF residues 33-800 + calmodulin + cAMP<br />
[[1xfx]], [[1xfy]], [[1xfz]] - EF residues 33-800 + calmodulin


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:40, 8 January 2020


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

  • .
  • of EF. Water molecules are shown as red spheres.
  • 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


ReferencesReferences

  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