title: Prediction of the general structure of OmpF and PhoE from the sequence and structure of porin from Rhodobacter capsulatus. Orientation of porin in the membrane.
abstract: By comparing the hydrophilicity profiles and sequences of porin from Rhodobacter capsulatus with those of OmpF and PhoE from Escherichia coli, a set of insertions and deletions for alignment of the sequences has been deduced. With this alignment a similar folding of OmpF and PhoE has been predicted as found by X-ray structure analysis of porin from Rhodobacter capsulates. Furthermore, the orientation of the porin trimer in the outer membrane was inferred from topological data on PhoE. According to this result a single channel of approx. 30 A diameter starts at the outer surface. Near the middle of the outer membrane bilayer this channel branches out into three separate channels, each running within a single porin monomer to the periplasmic surface.
authors.affiliation: Institut für Biophysik und Strahlenbiologie, Albert-Ludwigs-Universität, Freiburg, Germany.
authors.forename: W
authors.initials: W
authors.lastname: Welte
authors.forename: M S
authors.initials: MS
authors.lastname: Weiss
authors.forename: U
authors.initials: U
authors.lastname: Nestel
authors.forename: J
authors.initials: J
authors.lastname: Weckesser
authors.forename: E
authors.initials: E
authors.lastname: Schiltz
authors.forename: G E
authors.initials: GE
authors.lastname: Schulz
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry; D008969:Molecular Sequence Data; D018272:Porins; D016354:Rhodobacter capsulatus / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D001425:Bacterial Outer Membrane Proteins; D018272:Porins