Structure of the human voltage-dependent anion channel

Bayrhuber, M; Meins, T; Habeck, M; Becker , S; Giller, K; Villinger , S; Vonrhein, C; Griesinger, C; Zweckstetter, M; Zeth, K

doi:10.1073/pnas.0808115105

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Structure of the human voltage-dependent anion channel

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Habeck, M
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., et al. (2008). Structure of the human voltage-dependent anion channel. Proceedings of the National Academy of Sciences of the United States of America, 105(40), 15370-15375. doi:10.1073/pnas.0808115105.

Cite as: https://hdl.handle.net/21.11116/0000-000B-25C3-F

Abstract

The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a amp;946;-barrel architecture composed of 19 amp;946;-strands with an amp;945;-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.