Cited by 588Mitochondrial Function and PathologyProtein Structure and DynamicsEnzyme Structure and Function

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Structure of the human voltage-dependent anion channel

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Bayrhuber, Monika, Meins, Thomas, Habeck, Michael, Becker, Stefan, Giller, Karin, Villinger, Saskia, Vonrhein, Clemens, Griesinger, Christian, Zweckstetter, Markus, Zeth, Kornelius·2008·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0808115105PMC PMC2557026

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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 β-barrel architecture composed of 19 β-strands with an α-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.

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Authors: Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., & Zeth, K.
Affiliations: Max Planck Institute for Biophysical Chemistry (DE)
Max Planck Institute of Biochemistry (DE)
Max Planck Institute for Developmental Biology (DE)
Global Phasing (United Kingdom) (GB)
ORCID: Bayrhuber, Monika
Habeck, Michael
Becker, Stefan
Giller, Karin
Vonrhein, Clemens
Griesinger, Christian
Zweckstetter, Markus
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2008-10-07
Volume: 105
Issue: 40
Pages: 15370-15375
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0808115105
PMC: PMC2557026
OpenAlex: W2134087185
Cited by: 588
References: 37
Citations by year: 2026: 17 · 2025: 23 · 2024: 35 · 2023: 27 · 2022: 26 · 2021: 43 · 2020: 39 · 2019: 24 · 2018: 29 · 2017: 29 · 2016: 44 · 2015: 30 · 2014: 40 · 2013: 21 · 2012: 41
FWCI: 16.47
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
DORA PSI (Paul Scherrer Institute) (submittedVersion)
Max Planck Institute for Plasma Physics (submittedVersion)
GRO (submittedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
Funders: Deutsche Forschungsgemeinschaft (ZW 71/2-1)
Max-Planck-Gesellschaft
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: voltage-dependent anion channel, VDAC1, mitochondrial outer membrane, protein structure, Tom40, mitochondrial apoptosis, metabolic flux
MeSH terms: Humans, Models, Molecular, Protein Structure, Secondary, Crystallography, X-Ray, Dimerization, Nuclear Magnetic Resonance, Biomolecular, Voltage-Dependent Anion Channel 1, Hydrophobic and Hydrophilic Interactions

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Structure of the human voltage-dependent anion channel

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