Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.
In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.
D000577:Amides / Q000032:analysis; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D002850:Chromatography, Gel; D003488:Cyanogen Bromide; D004926:Escherichia coli / Q000032:analysis; D008565:Membrane Proteins; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin; D014364:Tryptophan / Q000032:analysis
D000577:Amides; D001425:Bacterial Outer Membrane Proteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D014364:Tryptophan; D014357:Trypsin; D003488:Cyanogen Bromide