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  Voltage dependence of conformational dynamics and subconducting states of VDAC-1.

Briones, R., Weichbrodt, C., Paltrinieri, L., Mey, I., Villinger, S., Giller, K., et al. (2016). Voltage dependence of conformational dynamics and subconducting states of VDAC-1. Biophysical Journal, 111(6), 1223-1234. doi:10.1016/j.bpj.2016.08.007.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-81A5-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-9C18-C
Genre: Journal Article

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 Creators:
Briones, R.1, Author              
Weichbrodt, C., Author
Paltrinieri, L., Author
Mey, I., Author
Villinger, S., Author
Giller, K.2, Author              
Lange, A., Author
Zweckstetter, M.3, Author              
Griesinger, C.2, Author              
Becker, S.2, Author              
Steinem, C., Author
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondrial membrane that transports energy metabolites and is involved in apoptosis. The available structures of VDAC proteins show a wide β-stranded barrel pore, with its N-terminal α-helix (N-α) bound to its interior. Electrophysiology experiments revealed that voltage, its polarity, and membrane composition modulate VDAC currents. Experiments with VDAC-1 mutants identified amino acids that regulate the gating process. However, the mechanisms for how these factors regulate VDAC-1, and which changes they trigger in the channel, are still unknown. In this study, molecular dynamics simulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationships of an "open" channel and they also show several subconducting transient states that are more cation selective in the simulations. We observed voltage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged amino acids. We constructed conformational models of the protein voltage response and the pore changes that consistently explain the protein conformations observed at opposite voltage polarities, either in phosphatidylethanolamine or phosphatidylcholine membranes. The submicrosecond VDAC-1 voltage response shows intrinsic structural changes that explain the role of key gating amino acids and support some of the current gating hypotheses. These voltage-dependent protein changes include asymmetric barrel distortion, its interaction with the membrane, and significant displacement of N-α amino acids.

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Language(s): eng - English
 Dates: 2016-09-20
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2016.08.007
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 111 (6) Sequence Number: - Start / End Page: 1223 - 1234 Identifier: -