|
| YaxAB |
 |
Both YaxA and YaxB are required for cytotoxic activity. Structural homology of YaxA are pore-forming toxins HblB (from Bacillus cereus) and HlyE (from E. coli). YaxA PDB code: 6EK7. YaxB PDB code: 6EK8. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
| Aerolysin |
|
PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
| | | |
