The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating

• DOI: 10.1073/pnas.0809634105
• Publication Date: 2008-11-07T02:25:48Z
• Authors: Rachna Ujwal; Duilio Cascio; Jacques-Philippe ...; Salem Faham; Jun Zhang; Ligia Toro; Peipei Ping; Jeff Abramson
• Keywords: Voltage-dependent anion channel; VDAC1; Organelle

The voltage-dependent anion channel (VDAC) constitutes the major pathway for entry and exit of metabolites across outer membrane mitochondria can serve as a scaffold molecules that modulate organelle. We report crystal structure beta-barrel eukaryotic protein, murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing high-resolution image its architecture formed by 19 beta-strands. Unlike recent NMR human VDAC1, position voltage-sensing N-terminal segment is clearly resolved. alpha-helix oriented against interior wall, causing partial narrowing center pore. This ideally positioned to regulate conductance ions passing through VDAC