Molecular characterization of the gene coding for major outer membrane protein OmpA from Enterobacter aerogenes
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The ompA gene from Salmonella typhimurium, encoding a major heat-modifiable protein of the outer membrane, has been cloned and extensively characterized. When expressed in Escherichia coli the gene directs the synthesis of an OmpA protein which is function ...
The secondary structure of porin, maltoporin, and OmpA protein reconstituted in lipid membranes was detd. by Raman spectroscopy. The 3 proteins have similar structures consisting of 50-60% b-strand, .apprx.20% b-turn, and
The cloned ompA gene from Serratia marcescens was fully expressed in Escherichia coli and its product correctly assembled into the outer membrane. The S. marcescens polypeptide was not functionally equivalent to the E. coli OmpA protein, which serves as a ...
The molecular organization of the malT region of the Escherichia coli K-12 chromosome has been elucidated by nucleotide sequence studies. A single open reading frame of 901 codons comprises the malT gene which is separated by a repetitive extragenic palind ...
The 325-residue OmpA protein is one of the major outer membrane proteins of Escherichia coli. It serves as the receptor for several T-even-like phages and is required for the action of certain colicins and for the stabilization of mating aggregates in conj ...
