Crystallization and preliminary X-ray crystallographic studies of human voltage-dependent anion channel isoform I (HVDAC1).
The major channel by which metabolites can pass through the outer mitochondrial membrane is formed by the voltage-dependent anion-channel (VDAC) family. Functionally, VDAC is involved in the limited exchange of ATP, ADP and small hydrophilic molecules across the outer membrane. Moreover, there is compelling evidence that VDAC isoforms in mammals may act in the cross-talk between mitochondria and the cytoplasm by direct interaction with enzymes involved in energy metabolism and proteins involved in mitochondrial-induced apoptosis. To obtain a high-resolution structure of this channel, human VDAC protein isoform I was overproduced in Escherichia coli. After refolding and testing the correct fold using circular dichroism, a subsequent broad-range screening in different detergents resulted in a variety of crystals which diffracted to 3.5 A resolution. The crystal lattice belongs to the trigonal space group P321, with unit-cell parameters a = 78.9, c = 165.7 A and one monomer in the asymmetric unit.
Meins
Thomas
T
Max Planck Institute of Biochemistry, Department of Membrane Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Vonrhein
Clemens
C
Zeth
Kornelius
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D051336:Mitochondrial Membranes / Q000737:chemistry; D017510:Protein Folding; D020033:Protein Isoforms / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D050995:Voltage-Dependent Anion Channel 1 / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D020033:Protein Isoforms; C494762:VDAC1 protein, human; D050995:Voltage-Dependent Anion Channel 1