A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency inEscherichia coliK-12
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چکیده
منابع مشابه
Study of the immunogenicity of outer membrane protein A (ompA) gene from Acinetobacter baumannii as DNA vaccine candidate in vivo
Objective(s): Acinetobacter baumannii is one the most dangerous opportunistic pathogens in hospitalized infections. This bacterium is resistant to 90% of commercial antibiotics. Therefore, developing new strategies to cure A. baumannii-infections is urgent. The DNA vaccines new approach in which the immunogen can be directly expressed inside the target cells through cl...
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 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 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...
متن کاملAssembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12.
TolC is a multifunctional outer membrane protein of Escherichia coli that folds into a novel alpha-beta-barrel conformation absent in the other model outer membrane proteins used in assembly studies. The data presented in this work show that the unique folded structure of TolC reflects a unique assembly pathway. During its assembly, the newly translocated nascent TolC monomers are released in t...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1987
ISSN: 0014-5793
DOI: 10.1016/0014-5793(87)80324-1