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Journal Article

Beta-barrel mobility underlies closure of the voltage-dependent anion channel.

MPS-Authors
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Zachariae,  U.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Schneider,  R.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Briones,  R.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Gattin,  Z.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

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Demers,  J. P.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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de Groot,  B. L.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Lange,  A.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://ac.els-cdn.com/S0969212612002493/1-s2.0-S0969212612002493-main.pdf?_tid=7373c392-fcce-11e1-91ef-00000aab0f6c&acdnat=1347450122_5973873033108dc948eda5eae0cde7f4
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Fulltext (public)

1481428.pdf
(Publisher version), 4MB

Supplementary Material (public)

1481428_Supplement.pdf
(Supplementary material), 358KB

Citation

Zachariae, U., Schneider, R., Briones, R., Gattin, Z., Demers, J. P., Giller, K., et al. (2012). Beta-barrel mobility underlies closure of the voltage-dependent anion channel. Structure, 20(9), 1540-1549. doi:10.1016/j.str.2012.06.015.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-A67C-D
Abstract
The voltage-dependent anion channel (VDAC) is the major protein in the outer mitochondrial membrane, where it mediates transport of ATP and ADP. Changes in its permeability, induced by voltage or apoptosis-related proteins, have been implicated in apoptotic pathways. The three-dimensional structure of VDAC has recently been determined as a 19-stranded β-barrel with an in-lying N-terminal helix. However, its gating mechanism is still unclear. Using solid-state NMR spectroscopy, molecular dynamics simulations, and electrophysiology, we show that deletion of the rigid N-terminal helix sharply increases overall motion in VDAC's β-barrel, resulting in elliptic, semicollapsed barrel shapes. These states quantitatively reproduce conductance and selectivity of the closed VDAC conformation. Mutation of the N-terminal helix leads to a phenotype intermediate to the open and closed states. These data suggest that the N-terminal helix controls entry into elliptic β-barrel states which underlie VDAC closure. Our results also indicate that β-barrel channels are intrinsically flexible.