Abstract
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. After decades of trials, three groups independently reported the 3D structure of this eukaryotic membrane protein consisting of a 19-stranded β-barrel. Our group resolved the mVDAC1 structure at 2.3Å resolution revealing a high-resolution image of its architecture including the position of the voltage sensing N-terminal α-helix segment- oriented against the interior wall causing a partial narrowing at the center of the pore.
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