The Crystal Structure of Mouse VDAC1 at 2.3 Å Resolution Reveals Mechanistic Insights into Metabolite Gating

The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a β-barrel eukaryotic membrane protei...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-11, Vol.105 (46), p.17742-17747
Main Authors: Ujwal, Rachna, Cascio, Duilio, Colletier, Jacques-Philippe, Faham, Salem, Zhang, Jun, Toro, Ligia, Ping, Peipei, Abramson, Jeff
Format: Article
Language:English
Subjects:
Amino acids
Animals
ANIONS
ARCHITECTURE
Biological Sciences
CRYSTAL STRUCTURE
Crystallization
Crystallography, X-Ray
Electric potential
Ion Channel Gating
Ions
MATERIALS SCIENCE
MEMBRANE PROTEINS
MEMBRANES
Metabolism
METABOLITES
Mice
MITOCHONDRIA
Models, Molecular
Molecular structure
Molecules
Physiological regulation
Porosity
Protein metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
RESOLUTION
Rodents
Solubility
Static Electricity
Voltage dependent anion channels
Voltage-Dependent Anion Channel 1 - chemistry
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Summary:The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a β-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 Å resolution, revealing a high-resolution image of its architecture formed by 19 β-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The α-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0809634105