Open AccessCrystallization and preliminary X‐ray crystallographic studies of human voltage‐dependent anion channel isoform I (HVDAC1)
Author(s) -
Meins Thomas,
Vonrhein Clemens,
Zeth Kornelius
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910801676x
Subject(s) - voltage dependent anion channel , gene isoform , bacterial outer membrane , cytoplasm , crystallization , crystallography , chemistry , ion channel , crystal structure , ion , biophysics , biochemistry , escherichia coli , biology , gene , receptor , organic chemistry
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 Å resolution. The crystal lattice belongs to the trigonal space group P 321, with unit‐cell parameters a = 78.9, c = 165.7 Å and one monomer in the asymmetric unit.