Models for the structure of outer-membrane proteins of Escherichia coli derived from raman spectroscopy and prediction methods.
The secondary structure of porin, maltoporin and OmpA protein reconstituted in lipid membranes is determined by Raman spectroscopy. The three proteins have similar structures consisting of 50 to 60% beta-strand, about 20% beta-turn, and less than 15% alpha-helix. Employing a method for structural prediction that accounts for amphipathic beta-strands, folding models are developed for porin and for the segment of OmpA protein incorporated into the membrane. In the model, the OmpA fragment consists of eight amphipathic membrane-spanning beta-strands that form a beta-barrel. Similarly, porin is folded into ten amphipathic membrane-spanning beta-strands that are located at the surface of the trimer towards the lipids and eight predominantly hydrophilic strands in the interior.
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D004926:Escherichia coli / Q000032:analysis*; D008954:Models, Biological; D009943:Organophosphorus Compounds; D018272:Porins; D011487:Protein Conformation; D011991:Receptors, Virus; D013059:Spectrum Analysis, Raman
D001425:Bacterial Outer Membrane Proteins; D009943:Organophosphorus Compounds; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins; C008705:octamethyl pyrophosphoramide