Regulation of the OmpA outer membrane protein of Escherichia coli
نویسندگان
چکیده
منابع مشابه
Membrane 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...
متن کاملPrimary 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 کاملPseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein.
A Pseudomonas aeruginosa outer membrane protein F-deficient omega-insertion mutant strain H636, in contrast to its protein F-sufficient parent strain H103, was unable to grow on unsupplemented Proteose Peptone no. 2 broth (Difco Laboratories, Detroit, Mich.). Addition of high concentrations of NaCl, KCl, glucose, sucrose, or potassium succinate permitted growth of strain H636 at rates approachi...
متن کاملAn outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export.
Pulse-chase experiments were performed to follow the export of the Escherichia coli outer membrane protein OmpA. Besides the pro-OmpA protein, which carries a 21-residue signal sequence, three species of ompA gene products were distinguishable. One probably represented an incomplete nascent chain, another the mature protein in the outer membrane, and the third, designated imp-OmpA (immature pro...
متن کاملSecondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa.
When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate. This result suggests that the proteins fold in a similar manner, with an N-terminal, membrane-spanning beta-barrel domain and a C-terminal, globular, periplasmic domain.
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.147.3.972-985.1981