title: Do small headgroups of phosphatidylethanolamine and phosphatidic acid lead to a similar folding pattern of the K(+) channel?
abstract: Phospholipid headgroups act as major determinants in proper folding of oligomeric membrane proteins. The K(+)-channel KcsA is the most popular model protein among these complexes. The presence of zwitterionic nonbilayer lipid phosphatidylethanolamine (PE) is crucial for efficient tetramerization and stabilization of KcsA in a lipid bilayer. In this study, the influence of PE on KcsA folding properties was analyzed by tryptophan fluorescence and acrylamide quenching experiments and compared with the effect of anionic phosphatidic acid (PA). The preliminary studies suggest that the small size and hydrogen bonding capability of the PE headgroup influences KcsA folding via a mechanism quite similar to that observed for anionic PA.
authors: Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. mraja@pmcol.ualberta.ca
authors: Mobeen
authors: M
authors: Raja
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D008051:Lipid Bilayers / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D010712:Phosphatidic Acids / Q000737:chemistry*; D010714:Phosphatidylethanolamines / Q000737:chemistry*; D015221:Potassium Channels / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding / Q000187:drug effects
chemical_list: D001426:Bacterial Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010712:Phosphatidic Acids; D010714:Phosphatidylethanolamines; D015221:Potassium Channels; C107790:prokaryotic potassium channel; C483858:phosphatidylethanolamine