Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
|Abstract||Potassium channels allow the selective flow of K(+) ions across membranes. In response to external gating signals, the potassium channel can move reversibly through a series of structural conformations from a closed to an open state. 2D crystals of the inwardly rectifying K(+) channel KirBac3.1 from Magnetospirillum magnetotacticum have been captured in two distinct conformations, providing "snap shots" of the gating process. Analysis by electron ... [truncated at 450 characters in length]|
|Author||Kuo, Anling; Domene, Carmen; Johnson, Louise N; et al|
|Subject||Amino Acid Sequence Amino Acids, Aromatic Cloning, Molecular Cryoelectron Microscopy Crystallography, X-Ray DNA, Bacterial Dimerization Lipid Bilayers Magnetospirillum Models, Molecular Molecular Sequence Data Potassium Channels, Inwardly Rectifying Protein Conformation Protein Structure, Quaternary Protein Structure, Secondary Sequence Homology, Amino Acid chemistry genetics chemistry ultrastructure|
A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type 10 is required for mitochondrial integrity and cell survival.
|Abstract||Deficiency of the mitochondrial enzyme 2-methyl-3-hydroxybutyryl-CoA dehydrogenase involved in isoleucine metabolism causes an organic aciduria with atypical neurodegenerative course. The disease-causing gene is HSD17B10 and encodes 17beta-hydroxysteroid dehydrogenase type 10 (HSD10), a protein also implicated in the pathogenesis of Alzheimer's disease. Here we show that clinical symptoms in patients are not correlated with residual enzymatic act ... [truncated at 450 characters in length]|
|Author||Rauschenberger, Katharina; Schöler, Katja; Sass, Jörn Oliver; et al|
|Subject||3-Hydroxyacyl CoA Dehydrogenases Animals Apoptosis Cell Survival Cells, Cultured Fibroblasts Gene Deletion Genetic Complementation Test Humans Hydroxysteroid Dehydrogenases Infant Mice Mice, Knockout Mitochondria Models, Molecular Neurons Protein Structure, Tertiary Xenopus deficiency metabolism metabolism ultrastructure deficiency metabolism physiology ultrastructure physiology|