Secondary Structure Edit
Secondary structure was predicted using PredictProtein. The results indicate a mostly helical structure (about 75%) with few loops and even fewer beta strands. The solvent accesibility predictor indicated the molecule has 37% buried sequences, 47% exposed sequences, and 16% intermediate sequences.
Tertiary StructureEditThe tertiary structure of anthrax lethal factor has been extensively studied primarily to understand its substrate binding to aid drug development. Research indicates very similar tertiary and quaternary structures of lethal factor. There are four distinct domains that each play an integral role in the proteins' toxic effects. Although the domains can be identified based on their funciton, location, and composition, the protein is a single folden unit. Nonetheless the folded protein contains a zinc ion (in the fourth domain) catagorizing the protein as a metalloproteinase. The ion is organized tetrahedrally from a water molecule that can act as protinator for a leaving group after catalysis. A large groove (40 angstroms), which is located in close proximity to the zink ion, acts as the active site for substrate binding. The groove is a combination of side chains from domains two, three, and four.
- Patrick: Anthrax Toxin: Introduction
- Patrick: Anthrax Toxin: Biological Function
- Patrick: Anthrax Toxin: Biosynthesis
- Patrick: Anthrax Toxin: Gene Sequence
- Patrick: Anthrax Toxin: Amino Acid Sequence and Composition
- Patrick: Anthrax Toxin: Secondary and Tertiary Structure
- Patrick: Anthrax Toxin: Domains and Structural Motifs
- Patrick: Anthrax Toxin: Interactions with macromolecules and small molecules
- Patrick: Anthrax Toxin: Molecular biodiversity and evolution
- Patrick: Anthrax Toxin: PyMOL Images
- Patrick: Anthrax Toxin: Literature Review
- Patrick: Anthrax Toxin: Useful online resources
Anthrax Lethal Factor Domains and General Overview . Proteopedia.org
Pannifer AD et al. 2001. Crystal Structure of the Anthrax Lethal Factor .Nature. 414 (6860): 229-33.