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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, 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]
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- This work was supported by NIH roadmap grant GM075879. Purchase operation and maintenance of instruments used were supported by NIH grants GM066360 GM47467 and EB002026. S.H. was supported by the Swiss National Science Foundation. V.Y.O. was supported by the Wenner-Gren Foundation Stockholm. Initial research on this project was supported by the Ludwig Foundation for Cancer Research. We thank V. Gelev from FBReagents.com Cambridge Massachusetts for custom synthesis of the 2 H-LDAO; S. Samanta for help with the electrophysiological measurements; and D. Frueh A. Koglin Z.-Y. J. Sun K. Oxenoid and S. Jenni for technical help and valuable discussions. The atomic coordinates of VDAC-1 in LDAO micelles have been deposited at the Protein Data Bank with code 2k4t.
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Metadata
- 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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