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Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15370-5. doi: 10.1073/pnas.0808115105. Epub 2008 Oct 1.

Structure of the human voltage-dependent anion channel.

Author information

1
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

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 beta-barrel architecture composed of 19 beta-strands with an alpha-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.

PMID:
18832158
PMCID:
PMC2557026
DOI:
10.1073/pnas.0808115105
[Indexed for MEDLINE]
Free PMC Article

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