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

Zachariae, U.; Schneider, R.; Briones, R.; Gattin, Z.; Demers, J. P.; Giller, K.; Maier, E.; Zweckstetter, M.; Griesinger, C.; Becker, S.; Benz, R.; de Groot, B. L.; Lange, A.

doi:10.1016/j.str.2012.06.015

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

MPS-Authors

/persons/resource/persons16069

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

/persons/resource/persons15783

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

/persons/resource/persons31221

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

/persons/resource/persons36441

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

/persons/resource/persons14974

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

/persons/resource/persons36496

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

/persons/resource/persons16093

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

/persons/resource/persons15147

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

/persons/resource/persons14824

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

/persons/resource/persons14970

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

/persons/resource/persons15414

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

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1481428.pdf
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1481428_Supplement.pdf
(付録資料), 358KB

引用

Zachariae, U., Schneider, R., Briones, R., Gattin, Z., Demers, J. P., Giller, K., Maier, E., Zweckstetter, M., Griesinger, C., Becker, S., Benz, R., de Groot, B. L., & Lange, A. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-000F-A67C-D

要旨

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.