1TZN

Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore bound to the VWA domain of CMG2, an anthrax toxin receptor

Summary for 1TZN

• Entry DOI: 10.2210/pdb1tzn/pdb
• Related: 1SHT 1TZO
• Descriptor: Protective antigen, Anthrax toxin receptor 2, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: heptamer, toxin receptor-toxin complex, toxin receptor/toxin
• Biological source: Bacillus anthracis str.; More
• Cellular location: Secreted, extracellular space: P13423; Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Isoform 3: Secreted: P58335
• Total number of polymer chains: 28
• Total formula weight: 1161499.70

Authors

Lacy, D.B.,Wigelsworth, D.J.,Melnyk, R.A.,Collier, R.J. (deposition date: 2004-07-10, release date: 2004-08-17, Last modification date: 2024-04-03)

Primary citation

Lacy, D.B.,Wigelsworth, D.J.,Melnyk, R.A.,Harrison, S.C.,Collier, R.J.
Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation
Proc.Natl.Acad.Sci.USA, 101:13147-13151, 2004

PubMed Abstract: 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.

PubMed: 15326297
DOI: 10.1073/pnas.0405405101

Experimental method

X-RAY DIFFRACTION (4.3 Å)