Structure of the mitochondrial outer membrane channel derived from electron microscopy of 2D crystals.
A structural model for the channel in the mitochondrial outer membrane is presented, derived from electron microscopic studies of two-dimensional crystals and inferences from the primary structure of the 30-kDa polypeptide which forms the channel. The channel is represented as a cylindrical beta-barrel, with a carbon backbone diameter of 3.8 nm. The axial projection of the cylinder is divided radially into four sectors by four interchannel contact points. These sectors are characterized in terms of their interactions with lipid and macromolecular ligands, and in terms of the presence or absence of exposed basic amino acids.
Mannella
C A
CA
Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509.
D003460:Crystallization; D007091:Image Processing, Computer-Assisted; D007425:Intracellular Membranes / Q000648:ultrastructure; D007473:Ion Channels / Q000648:ultrastructure*; D008565:Membrane Proteins; D008854:Microscopy, Electron; D008928:Mitochondria / Q000648:ultrastructure*; D008961:Models, Structural; D009491:Neurospora / Q000648:ultrastructure; D018272:Porins; D050994:Voltage-Dependent Anion Channels
D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels