Anthrax edema factor

spinqualitylabelsall models 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). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Anthrax edema factor (EF) is an enzyme which is part of the Bacillus anthracis anthrax toxin. The full 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. The binding of calmodulin to EF changes it from its non-active form to the active one. 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).

3D structures of anthrax edema factor

Updated on 07-May-2018

1pk0 – EF adenylate cyclase domain C terminal + calmodulin + anthraniloyl-deoxy-ATP
1pk0 - EF adenylate cyclase domain C terminal + calmodulin + phosphonylmethoxyethyl-ADP
1s26 - EF adenylate cyclase domain C terminal + calmodulin + methylene-ATP
1sk6 - EF adenylate cyclase domain C terminal + calmodulin + pyrophosphate + cAMP
1xfu - EF (mutant) + calmodulin
1xfv - EF + calmodulin + deoxy-ATP
1xfw - EF + calmodulin + cAMP
1xfx, 1xfy, 1xfz - EF + calmodulin

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Michal Harel, Alexander Berchansky