1tzn
Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore bound to the VWA domain of CMG2, an anthrax toxin receptor
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| , resolution 4.30Å | |||||||
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| Ligands: | , | ||||||
| Gene: | pagA (Bacillus anthracis), ANTXR2 (Homo sapiens) | ||||||
| Related: | 1SHT, 1TZO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Fibromatosis, juvenile hyaline OMIM:[608041], Hyalinosis, infantile systemic OMIM:[608041]
About this StructureAbout this Structure
1TZN is a Protein complex structure of sequences from Bacillus anthracis and Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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