Major heat-modifiable outer membrane protein in gram-negative bacteria: comparison with the ompA protein of Escherichia coli
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چکیده
منابع مشابه
Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.
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...
متن کاملOuter membrane protein biogenesis in Gram-negative bacteria
Gram-negative bacteria contain a double membrane which serves for both protection and for providing nutrients for viability. The outermost of these membranes is called the outer membrane (OM), and it contains a host of fully integrated membrane proteins which serve essential functions for the cell, including nutrient uptake, cell adhesion, cell signalling and waste export. For pathogenic strain...
متن کاملThe heat-modifiable outer membrane protein of Actinobacillus actinomycetemcomitans: relationship to OmpA proteins.
The outer membrane of Actinobacillus actinomycetemcomitans contains a 29-kDa protein which exhibits heat modifiability on sodium dodecyl sulfate-polyacrylamide gels and represents a major target for immunoglobulin G antibody in sera of periodontitis patients colonized by this organism. In the present study, the N-terminal amino acid sequence of the 29-kDa outer membrane protein was determined a...
متن کاملRole of a major outer membrane protein in Escherichia coli.
Mutants of Escherichia coli B/r lacking a major outer membrane protein, protein b, were obtained by selecting for resistance to copper. These mutants showed a decreased ability to utilize a variety of metabolites when the metabolites were present at low concentrations. Also, mutants of E. coli K-12 lacking proteins b and c from the outer membrane were shown to have an identical defect in the up...
متن کاملMembrane assembly of the outer membrane protein OmpA of Escherichia coli.
The membrane part (residues 1 to approximately 170) of the 325-residue Escherichia coli outer membrane protein OmpA is thought to exist in the membrane as an 8-stranded beta-barrel, subdividing this part into four segments. The influence of proline residues on membrane assembly of the protein has been studied. These were introduced, using site-directed mutagenesis, into each of seven of the ant...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1980
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.143.2.906-913.1980