title: An alternative topological model for Escherichia coli OmpA.
abstract: The current topological model for the Escherichia coli outer membrane protein OmpA predicts eight N-terminal transmembrane segments followed by a long periplasmic tail. Several recent reports have raised serious doubts about the accuracy of this prediction. An alternative OmpA model has been constructed using (1) computer-aided predictions developed specifically to predict topology of bacterial outer membrane porins, (2) the results of two reports that identified sequence homologies between OmpA and other peptidoglycan-associated proteins, and (3) biochemical, immunochemical, and genetic topological data on proteins of the OmpA family provided by numerous previous studies. The new model not only agrees with the varied experimental data concerning OmpA but also provides an improved understanding of the relationship between the structure and the multifunctional role of OmpA in the bacterial outer membrane.
authors.affiliation: Department of Microbiology, University of Texas, Austin 78712, USA.
authors.forename: C
authors.initials: C
authors.lastname: Stathopoulos
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001425:Bacterial Outer Membrane Proteins