期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 122, 期 45, 页码 10296-10305出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.8b08304
关键词
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资金
- NIH [GM59796]
- Welch grant [F1896]
- Defense Threat Reduction Agency-Joint Science and Technology Office for Chemical and Biological Defense (IAA) [DTRTA10027IA-3167]
- U.S. Department of Energy's National Nuclear Security Administration [DE-NA-0003525]
- U.S. DOE's Office of Science [DE-AC52-06NA25396]
Anthrax toxin consists of a cation channel and two protein factors. Translocation of the anthrax protein factors from endosomal to the cytosolic compartment is a complex process which utilizes the cation channel. An atomically detailed understanding of the function of the anthrax translocation machinery is incomplete. We report atomically detailed simulations of the lethal factor and channel mutants. Kinetic and thermodynamic properties of early events in the trans location process are computed within the Milestoning theory and algorithm. Several mutants of the channel illustrate that long-range electrostatic interactions provide the dominant driving force for translocation. No external energy input is required because the lower pH in the endosome relative to the cytosol drives the initial translocation process forward. Channel mutants with variable sizes cause smaller effects on translocation events relative to charge manipulations. Comparison with available experimental data is provided.
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