Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin
نویسندگان
چکیده
منابع مشابه
Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin.
Deep rought mutants, which produce very defective lipopolysaccharides, are unable to export normal levels of porins into the outer membrane. In this study, we showed that lipopolysaccharides from such mutants were also unable to facilitate the trimerization, in vitro, of monomeric OmpF porin secreted by spheroplasts of Escherichia coli B/r. In contrast, lipopolysaccharides containing most or al...
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The assembly of outer membrane proteins of Escherichia coli was examined using the OmpF porin as a model. Since this protein is made as a precursor, which is processed to a protein of Mr 37,000 before being assembled into trimers in the outer membrane, we synthesized a modified OmpF, which lacked 16 out of 22 amino acid residues from its signal sequence, in a coupled transcription-translation s...
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The mechanism of uptake of aminoglycosides across the outer membrane of Escherichia coli was reevaluated. Porin-deficient mutants showed no alteration in gentamicin or kanamycin susceptibility. Furthermore, the influence of kanamycin on intrinsic tryptophan fluorescence of porin OmpF (Y. Kobayashi, and T. Nakae, Eur. J. Biochem. 151:231-236, 1985) was shown to be strongly influenced by protein ...
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Background and Aim: Salmonella Typhi belongs to the family Enterobacteriaceae, gram-negative bacilli and causes gastrointestinal diseases such as typhoid. This bacterium has a special structure and various genes, including the ompf gene (outer membrane protein). Recent studies have shown the possibility of using ompf in the development of a diagnostic tuberculosis vaccine. Therefore, the aim of...
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A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119-->Asp (G119D)] was identified in the internal loop L3 that contributes critically to the formation of the construction inside the lumen of the pore. X-ray structure analysis to a resolution of 3.0 A reveal...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1991
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.173.2.926-928.1991