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.

[1]  T. Wacker,et al.  Crystallization and preliminary X‐ray analysis of porin from Rhodobacter capsulatus , 1989, FEBS letters.

[2]  A. Engel,et al.  Localization of the lipopolysaccharides in metal-shadowed reconstituted lipid-porin membranes , 1990 .

[3]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.

[4]  G. Büldt,et al.  Densely packed β-structure at the protein-lipid interface of porin is revealed by high-resolution cryo-electron microscopy , 1989 .

[5]  B. Lugtenberg,et al.  Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12. , 1983, Journal of molecular biology.

[6]  R. Huber,et al.  A porin‐type protein is the main constituent of the cell envelope of the ancestral eubacterium Thermotoga maritima , 1990 .

[7]  F. Jähnig,et al.  Structure predictions of membrane proteins are not that bad. , 1990, Trends in biochemical sciences.

[8]  U. Henning,et al.  Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r. , 1982, The Biochemical journal.

[9]  W. Baumeister,et al.  Structure of the porin from a bacterial stalk , 1987, FEBS letters.

[10]  K. Gehring,et al.  Structural architecture of an outer membrane channel as determined by electron crystallography , 1991, Nature.

[11]  R. Benz,et al.  Permeation of hydrophilic molecules through the outer membrane of gram‐negativ bacteria , 1988 .

[12]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[13]  J. Rosenbusch,et al.  Porin channel triplets merge into single outlets in Escherichia coli outer membranes , 1985, Nature.

[14]  G. Schulz,et al.  The three‐dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution , 1990, FEBS letters.

[15]  R. H. Johnson.  THE ACCUMULATION OF OIL AND GAS IN SANDSTONE. , 1912, Science.

[16]  G. Schulz,et al.  Primary structure of porin from Rhodobacter capsulatus. , 1991, European journal of biochemistry.

[17]  M. Karplus,et al.  Crystallographic R Factor Refinement by Molecular Dynamics , 1987, Science.

[18]  G. Schulz,et al.  The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution , 1991, FEBS letters.

[19]  B. Lugtenberg,et al.  Role of the Arg158 residue of the outer membrane PhoE pore protein of Escherichia coli K 12 in bacteriophage TC45 recognition and in channel characteristics. , 1985, European journal of biochemistry.