Primary structure of porin from Rhodobacter capsulatus.
The primary structure of the integral membrane protein porin from the purple bacterium Rhodobacter capsulatus was determined. The protein was cleaved with trypsin, CNBr and Asp-N protease. The peptides were isolated, sequenced and aligned to a total length of 301 residues with an Mr of 31,536. The low isoelectric point of 3.9 is confirmed by the high excess of 34 Asp and 17 Glu (16.9%) over 10 Lys, 7 Arg and 2 His (6.3%). Overall sequence similarity to other porins is not evident when using sequence alignment programs. However, a partial relationship to Neisseria porins seems to exist. The established sequence has been used as the basis for a three-dimensional structure determination by X-ray diffraction at 0.18-nm resolution. The arrangement of the sequence in the 16-stranded beta-barrel of porin is given. Some sequence-structure correlations are discussed.
Schiltz
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E
Institut für Organische Chemie und Biochemie der Universität Freiburg, Federal Republic of Germany.
Kreusch
A
A
Nestel
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U
Schulz
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GE
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D018272:Porins; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000378:metabolism*; D014357:Trypsin
D001425:Bacterial Outer Membrane Proteins; D010446:Peptide Fragments; D018272:Porins; D014357:Trypsin; D003488:Cyanogen Bromide