
doi: 10.1007/bf02027309
pmid: 1689251
Structural information about the channel in the mitochondrial outer membrane, derived from sequence analysis and electron microscopy of two-dimensional crystals, is summarized. A model for the channel is presented, consisting of a cylindrical beta-barrel that is formed by one or two 30-kDa polypeptides, with an alpha-carbon backbone diameter of 3.8 nm. The radial distributions of basic amino acids and lipid-contact regions on the projected cylinder are mapped relative to interchannel bonding sites inferred from channel packing in the arrays. Speculation on the kinds of conformational changes that the channel might undergo is also presented.
Microscopy, Electron, Molecular Sequence Data, Membrane Proteins, Porins, Voltage-Dependent Anion Channels, Amino Acid Sequence, Intracellular Membranes, Plants, Ion Channels, Mitochondria
Microscopy, Electron, Molecular Sequence Data, Membrane Proteins, Porins, Voltage-Dependent Anion Channels, Amino Acid Sequence, Intracellular Membranes, Plants, Ion Channels, Mitochondria
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