PMID:7001461
| Citation |
Chen, R, Schmidmayr, W, Krämer, C, Chen-Schmeisser, U and Henning, U (1980) Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 77:4592-6 |
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| Abstract |
The amino acid sequence of major outer membrane protein II (ompA protein) from Escherichia coli K-12 has been determined. The transmembrane polypeptide consists of 325 residues, resulting in a molecular weight of 35,159. The transmembrane part of the protein is located between residues 1 and 177. In this part of the protein a predominantly lipophilic 27-residue segment exists that perhaps spans the membrane in a mostly alpha-helical conformation, or a 19-residue stretch of this segment might traverse the membrane linearly. Inside the outer membrane a sequence -Ala-Pro-Ala-Pro-Ala-Pro-Ala-Pro- exists that, analogous to the -Cys-Pro-Pro-Cys-Pro- sequence in the hinge region of immunoglobulin, could assume the conformation of a polyproline helix. Computer analysis did not reveal a clear overall pattern of internal homology in the protein; besides the -Ala-Pro- repeat, only one local area (two adjacent dodecapeptide segments) shows some repetitiveness. The same analysis did not produce evidence for internal homology in the previously determined sequence of outer membrane protein I (porin) nor was any marked resemblance detected between transmembrane proteins I and II. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Bacterial Outer Membrane Proteins/analysis; Bacterial Proteins; Escherichia coli/ultrastructure; Membrane Proteins/analysis; Peptide Fragments/analysis; Protein Conformation |
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