Limits...
Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry

View Article: PubMed Central - HTML - PubMed

ABSTRACT

Anthrax toxin is a tripartite complex in which the protective antigen moiety forms a pore through which lethal factor and edema factor are translocated. Fabre et al. reveal a mechanism for efficient translocation in their structure of the heptameric protective antigen prepore bound to three lethal factors.

No MeSH data available.


Related in: MedlinePlus

Resolution of the EM map and accuracy of model building. (A) Fourier shell correlation curve. According to the 0.5 forward scatter (FSC) criteria, the resolution of the final EM map is ∼15 Å. (B) Accuracy of LF docking in the EM map. Blue corresponds to low RMSD (0.85 Å) and red to high RMSD (4.39 Å). The overall average RMSD is 2.48 Å.
© Copyright Policy - openaccess
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC5037343&req=5

fig3: Resolution of the EM map and accuracy of model building. (A) Fourier shell correlation curve. According to the 0.5 forward scatter (FSC) criteria, the resolution of the final EM map is ∼15 Å. (B) Accuracy of LF docking in the EM map. Blue corresponds to low RMSD (0.85 Å) and red to high RMSD (4.39 Å). The overall average RMSD is 2.48 Å.

Mentions: After determining the contrast transfer function (CTF) using CTFIND3 (Mindell and Grigorieff, 2003), the final refinement was conducted with 36,823 particles using the Fourier reconstruction method of XMIPPv2.3 with the following settings: 20 refinements for each the angular sampling rate (10°, 8°, 5°, 3°, 2°, and 1°) with respective angular search of 1,000 (unlimited), 20, 15, 9, 6, and 3. No limit was set for the maximum change in origin offset. The search range for 5-D translational search was set at five pixels for the first four iterations and one pixel afterward. Low pass filtering was performed at each iteration at the resolution estimated using the FSC criteria of 0.6 (0.5 + 0.1). The resolution of the final map was estimated to be at 16-Å resolution (Fig. 3 A). Analysis of our current dataset with other software did not improve resolution. The final map was corrected for envelope function and CTF amplitude effects using the model derived from fitting the x-ray structures (Volkmann and Hanein, 1999).


Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry
Resolution of the EM map and accuracy of model building. (A) Fourier shell correlation curve. According to the 0.5 forward scatter (FSC) criteria, the resolution of the final EM map is ∼15 Å. (B) Accuracy of LF docking in the EM map. Blue corresponds to low RMSD (0.85 Å) and red to high RMSD (4.39 Å). The overall average RMSD is 2.48 Å.
© Copyright Policy - openaccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC5037343&req=5

fig3: Resolution of the EM map and accuracy of model building. (A) Fourier shell correlation curve. According to the 0.5 forward scatter (FSC) criteria, the resolution of the final EM map is ∼15 Å. (B) Accuracy of LF docking in the EM map. Blue corresponds to low RMSD (0.85 Å) and red to high RMSD (4.39 Å). The overall average RMSD is 2.48 Å.
Mentions: After determining the contrast transfer function (CTF) using CTFIND3 (Mindell and Grigorieff, 2003), the final refinement was conducted with 36,823 particles using the Fourier reconstruction method of XMIPPv2.3 with the following settings: 20 refinements for each the angular sampling rate (10°, 8°, 5°, 3°, 2°, and 1°) with respective angular search of 1,000 (unlimited), 20, 15, 9, 6, and 3. No limit was set for the maximum change in origin offset. The search range for 5-D translational search was set at five pixels for the first four iterations and one pixel afterward. Low pass filtering was performed at each iteration at the resolution estimated using the FSC criteria of 0.6 (0.5 + 0.1). The resolution of the final map was estimated to be at 16-Å resolution (Fig. 3 A). Analysis of our current dataset with other software did not improve resolution. The final map was corrected for envelope function and CTF amplitude effects using the model derived from fitting the x-ray structures (Volkmann and Hanein, 1999).

View Article: PubMed Central - HTML - PubMed

ABSTRACT

Anthrax toxin is a tripartite complex in which the protective antigen moiety forms a pore through which lethal factor and edema factor are translocated. Fabre et al. reveal a mechanism for efficient translocation in their structure of the heptameric protective antigen prepore bound to three lethal factors.

No MeSH data available.


Related in: MedlinePlus