Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
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The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with antiapoptotic proteins from the Bcl-2 family, and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the nuclear magnetic resonance (NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded β barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a beltlike fashion. In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid bilayers similar to those of the native protein. NMR measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-x L , for reduced β–nicotinamide adenine dinucleotide, and for cholesterol. Bcl-x L interacts with the VDAC barrel laterally at strands 17 and 18.
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It is unlikely that VDAC itself participates as a cholesterol channel, because the center of its ring-like structure is hydrophilic, suitable for anion transport but unsuitable for hydrophobic molecule transport.
“It is unlikely that VDAC itself participates as a cholesterol channel, as the center of its ring-like structure is hydrophilic, suitable for anion transport but unsuitable for hydrophobic molecule transport (103, 104).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [103]
The structural passages (page not provided) describe an open VDAC-1 barrel with an interior wall containing only two hydrophobic residues; they also report anion preference and cholesterol interaction sites on the barrel’s outside. These findings support the proposed rationale, but the paper does not test cholesterol passage or conclude that VDAC is unlikely to serve as a cholesterol channel. (LLM, conf=0.84)
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- Authors
- Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G.
- Affiliations
- Harvard University (US)
- Corresponding author
- Garces, Robert G.
- Malia, Thomas J.
- Wagner, Gerhard
- Venue
- Science
- Published
- 2008-08-29
- Volume
- 321
- Issue
- 5893
- Pages
- 1206-1210
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2579273
- OpenAlex
- W1986199954
- Cited by
- 667
- References
- 34
- Citations by year
- 2026: 13 · 2025: 16 · 2024: 23 · 2023: 21 · 2022: 21 · 2021: 45 · 2020: 35 · 2019: 29 · 2018: 39 · 2017: 38 · 2016: 51 · 2015: 37 · 2014: 53 · 2013: 40 · 2012: 49
- FWCI
- 21.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (P41GM066360, R01GM075879, GM 075879, GM-066360, GM47467, P01GM047467)
- National Institute of Biomedical Imaging and Bioengineering (EB 002026, P41EB002026)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- VDAC1, voltage-dependent anion channel, mitochondrial outer membrane, beta-barrel membrane proteins, detergent micelles, Bcl-xL, Bcl-2 family proteins, apoptosis, cholesterol binding, NAD+ binding, voltage-gated ion channels, protein solution structure
- MeSH terms
- Amino Acid Sequence, Binding Sites, Cholesterol, Detergents, Dimethylamines, Humans, Lipid Bilayers, Micelles, Molecular Sequence Data, NAD, Protein Conformation, Recombinant Proteins, Ion Channel Gating, Protein Structure, Secondary, Protein Folding, Nuclear Magnetic Resonance, Biomolecular, Voltage-Dependent Anion Channel 1, bcl-X Protein, Static Electricity, Hydrophobic and Hydrophilic Interactions
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