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.
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.
Welte
W
W
Institut für Biophysik und Strahlenbiologie, Albert-Ludwigs-Universität, Freiburg, Germany.
Weiss
M S
MS
Nestel
U
U
Weckesser
J
J
Schiltz
E
E
Schulz
G E
GE
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
D001425:Bacterial Outer Membrane Proteins; D018272:Porins