1tzo
From Proteopedia
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Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore
Overview
After binding to cellular receptors and proteolytic activation, the, protective antigen component of anthrax toxin forms a heptameric prepore., The prepore later undergoes pH-dependent conversion to a pore, mediating, translocation of the edema and lethal factors to the cytosol. We describe, structures of the prepore (3.6 A) and a prepore:receptor complex (4.3 A), that reveal the location of pore-forming loops and an unexpected, interaction of the receptor with the pore-forming domain. Lower pH is, required for prepore-to-pore conversion in the presence of the receptor, indicating that this interaction regulates pH-dependent pore formation. We, present an example of a receptor negatively regulating pH-dependent, membrane insertion.
About this Structure
1TZO is a Single protein structure of sequence from Bacillus anthracis with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation., Lacy DB, Wigelsworth DJ, Melnyk RA, Harrison SC, Collier RJ, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13147-51. Epub 2004 Aug 23. PMID:15326297
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