Membrane Association of the Diphtheria Toxin Translocation Domain Studied by Coarse-Grained Simulations and Experiment

Membrane Association of the Diphtheria Toxin Translocation Domain Studied by Coarse-Grained... compact and mostly retain globular structure. In the pres- ent work, we investigate how this refolded state interacts with membrane interfaces in the early steps of T-domain’s membrane association. Coarse-grained molecular dynam- ics simulations suggest two distinct membrane-bound conformations of the T-domain in the presence of bilayers composed of a mixture of zwitteronic and anionic phos- pholipids (POPC:POPG with a 1:3 molar ratio). Both membrane-bound conformations show a common near parallel orientation of hydrophobic helices TH8–TH9 rel- ative to the membrane plane. The most frequently observed membrane-bound conformation is stabilized by electrostatic interactions between the N-terminal segment Keywords Diphtheria toxin  Coarse-grained modeling of the protein and the membrane interface. The sec- Anionic lipids  Insertion  Low pH  Histidine protonation ond membrane-bound conformation is stabilized by Abbreviations T-domain Diphtheria toxin translocation domain CG Coarse-grained Electronic supplementary material The online version of this MD Molecular dynamics article (doi:10.1007/s00232-015-9771-3) contains supplementary POPC 1-Palmitoyl-2-oleoyl-phosphatidyl-choline material, which is available to authorized users. POPG 1-Palmitoyl-2-oleoyl-phosphatidyl-glycerol J. C. Flores-Canales  M. Kurnikova (&) COM Center of mass Department of Chemistry, Carnegie Mellon University, PMF Potential of mean force Pittsburgh, PA 15213, USA K Binding constant e-mail: kurnikova@cmu.edu K Partitioning coefficient M. Vargas-Uribe  http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Membrane Association of the Diphtheria Toxin Translocation Domain Studied by Coarse-Grained Simulations and Experiment

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Publisher
Springer US
Copyright
Copyright © 2015 by Springer Science+Business Media New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-015-9771-3
Publisher site
See Article on Publisher Site

Abstract

compact and mostly retain globular structure. In the pres- ent work, we investigate how this refolded state interacts with membrane interfaces in the early steps of T-domain’s membrane association. Coarse-grained molecular dynam- ics simulations suggest two distinct membrane-bound conformations of the T-domain in the presence of bilayers composed of a mixture of zwitteronic and anionic phos- pholipids (POPC:POPG with a 1:3 molar ratio). Both membrane-bound conformations show a common near parallel orientation of hydrophobic helices TH8–TH9 rel- ative to the membrane plane. The most frequently observed membrane-bound conformation is stabilized by electrostatic interactions between the N-terminal segment Keywords Diphtheria toxin  Coarse-grained modeling of the protein and the membrane interface. The sec- Anionic lipids  Insertion  Low pH  Histidine protonation ond membrane-bound conformation is stabilized by Abbreviations T-domain Diphtheria toxin translocation domain CG Coarse-grained Electronic supplementary material The online version of this MD Molecular dynamics article (doi:10.1007/s00232-015-9771-3) contains supplementary POPC 1-Palmitoyl-2-oleoyl-phosphatidyl-choline material, which is available to authorized users. POPG 1-Palmitoyl-2-oleoyl-phosphatidyl-glycerol J. C. Flores-Canales  M. Kurnikova (&) COM Center of mass Department of Chemistry, Carnegie Mellon University, PMF Potential of mean force Pittsburgh, PA 15213, USA K Binding constant e-mail: kurnikova@cmu.edu K Partitioning coefficient M. Vargas-Uribe 

Journal

The Journal of Membrane BiologySpringer Journals

Published: Feb 4, 2015

References

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