Structure of the human voltage-dependent anion channel.
The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a beta-barrel architecture composed of 19 beta-strands with an alpha-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.
Bayrhuber
Monika
M
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Meins
Thomas
T
Habeck
Michael
M
Becker
Stefan
S
Giller
Karin
K
Villinger
Saskia
S
Vonrhein
Clemens
C
Griesinger
Christian
C
Zweckstetter
Markus
M
Zeth
Kornelius
K
D018360:Crystallography, X-Ray; D019281:Dimerization; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D050995:Voltage-Dependent Anion Channel 1 / Q000737:chemistry* / Q000378:metabolism
C494762:VDAC1 protein, human; D050995:Voltage-Dependent Anion Channel 1