The published 3D structure of the VDAC channel: native or not?
The recently published 3D structures of the mitochondrial voltage-dependent anion-selective channel (VDAC) are almost identical to each other. However, they are in conflict with the results of biochemical and functional studies published in the past 18 years. Transmembrane folding patterns based on many biochemical and functional studies differ from the 3D structures in the exclusion of distinct transmembrane strands. These differences might be the consequence of changes observed in vitro that result in the formation of channels with the characteristic functional properties of VDAC. Is it possible to reconcile the discrepancies between the 3D structures and earlier models? As it was refolded from inclusion bodies, the protein used to obtain the 3D structures might not be in the native conformation. Here, I propose structural rearrangements that could occur spontaneously as a possible path to convert the 3D structure to my preferred biochemically determined native structure.
Colombini
Marco
M
Department of Biology, University of Maryland, College Park, MD 20742, USA. colombini@umd.edu
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D019809:Streptavidin / Q000737:chemistry / Q000378:metabolism; D050994:Voltage-Dependent Anion Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D050994:Voltage-Dependent Anion Channels; D019809:Streptavidin