- PDB-6uji: Low resolution crystal structure (5.5 A) of the anthrax toxin pro... -
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Entry
Database: PDB / ID: 6uji
Title
Low resolution crystal structure (5.5 A) of the anthrax toxin protective antigen heptamer prepore D425A mutant
Components
Protective antigen PA-63
Keywords
TOXIN / Anthrax Toxin / PA63 heptamer
Function / homology
Function and homology information
positive regulation of apoptotic process in another organism / host cell cytosol / negative regulation of MAPK cascade / Uptake and function of anthrax toxins / host cell endosome membrane / protein homooligomerization / toxin activity / host cell plasma membrane / extracellular region / identical protein binding ...positive regulation of apoptotic process in another organism / host cell cytosol / negative regulation of MAPK cascade / Uptake and function of anthrax toxins / host cell endosome membrane / protein homooligomerization / toxin activity / host cell plasma membrane / extracellular region / identical protein binding / membrane / metal ion binding Similarity search - Function
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
P30 GM110761
United States
Citation
Journal: J Mol Biol / Year: 2022 Title: Structure of the Anthrax Protective Antigen D425A Dominant Negative Mutant Reveals a Stalled Intermediate State of Pore Maturation. Authors: Harry Scott / Wei Huang / Kiran Andra / Sireesha Mamillapalli / Srinivas Gonti / Alexander Day / Kaiming Zhang / Nurjahan Mehzabeen / Kevin P Battaile / Anjali Raju / Scott Lovell / James G ...Authors: Harry Scott / Wei Huang / Kiran Andra / Sireesha Mamillapalli / Srinivas Gonti / Alexander Day / Kaiming Zhang / Nurjahan Mehzabeen / Kevin P Battaile / Anjali Raju / Scott Lovell / James G Bann / Derek J Taylor / Abstract: The tripartite protein complex produced by anthrax bacteria (Bacillus anthracis) is a member of the AB family of β-barrel pore-forming toxins. The protective antigen (PA) component forms an ...The tripartite protein complex produced by anthrax bacteria (Bacillus anthracis) is a member of the AB family of β-barrel pore-forming toxins. The protective antigen (PA) component forms an oligomeric prepore that assembles on the host cell surface and serves as a scaffold for binding of lethal and edema factors. Following endocytosis, the acidic environment of the late endosome triggers a pH-induced conformational rearrangement to promote maturation of the PA prepore to a functional, membrane spanning pore that facilitates delivery of lethal and edema factors to the cytosol of the infected host. Here, we show that the dominant-negative D425A mutant of PA stalls anthrax pore maturation in an intermediate state at acidic pH. Our 2.7 Å cryo-EM structure of the intermediate state reveals structural rearrangements that involve constriction of the oligomeric pore combined with an intramolecular dissociation of the pore-forming module. In addition to defining the early stages of anthrax pore maturation, the structure identifies asymmetric conformational changes in the oligomeric pore that are influenced by the precise configuration of adjacent protomers.
Resolution: 5.5→44.83 Å / Cor.coef. Fo:Fc: 0.898 / Cor.coef. Fo:Fc free: 0.873 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 1.587 Details: Rigid body refinement with B-factors set to the Wilson B-factor
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