3EMN

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

Summary for 3EMN

• Entry DOI: 10.2210/pdb3emn/pdb
• Descriptor: Voltage-dependent anion-selective channel protein 1, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• Functional Keywords: vdac1, eukaryotic membrane protein, beta barrel, channel, apoptosis, ion transport, mitochondrion, outer membrane, phosphoprotein, porin, transmembrane, transport, membrane protein
• Biological source: Mus musculus (Mouse)
• Cellular location: Isoform Mt-VDAC1: Mitochondrion outer membrane; Multi-pass membrane protein. Isoform Pl-VDAC1: Cell membrane; Multi-pass membrane protein: Q60932
• Total number of polymer chains: 1
• Total formula weight: 32873.88

Authors

Ujwal, R.,Cascio, D.,Colletier, J.-P.,Faham, S.,Zhang, J.,Toro, L.,Ping, P.,Abramson, J. (deposition date: 2008-09-24, release date: 2008-12-16, Last modification date: 2024-02-21)

Primary citation

Ujwal, R.,Cascio, D.,Colletier, J.P.,Faham, S.,Zhang, J.,Toro, L.,Ping, P.,Abramson, J.
The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating
Proc.Natl.Acad.Sci.USA, 105:17742-17747, 2008

PubMed 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. We report the crystal structure of a beta-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing a high-resolution image of its architecture formed by 19 beta-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The alpha-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.

PubMed: 18988731
DOI: 10.1073/pnas.0809634105

Experimental method

X-RAY DIFFRACTION (2.3 Å)