Isolation and characterization of recombinant OmpF-like porin from the Yersinia pseudotuberculosis outer membrane

The encoding sequence of the pore-forming OmpF-like protein from the Yersinia pseudotuberculosis outer membrane was cloned and expressed in Escherichia coli cells. Conditions for isolation and refolding of recombinant monomer and porin trimer were selected. Their spatial structures were characterize...

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Published inRussian journal of bioorganic chemistry Vol. 34; no. 2; pp. 162 - 168
Main Authors Khomenko, V A, Portnyagina, OYu, Novikova, O D, Isaeva, M P, Kim, NYu, Likhatskaya, G N, Vostrikova, O P, Solov'eva, T F
Format Journal Article
LanguageEnglish
Published 01.03.2008
Subjects
Escherichia coli
Yersinia pseudotuberculosis
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Summary:The encoding sequence of the pore-forming OmpF-like protein from the Yersinia pseudotuberculosis outer membrane was cloned and expressed in Escherichia coli cells. Conditions for isolation and refolding of recombinant monomer and porin trimer were selected. Their spatial structures were characterized by the intrinsic protein fluorescence and CD spectroscopy. It was shown that recombinant porins are similar in the composition of secondary structure elements to isolated porins, but have a considerably less compact tertiary structure. The pore-forming activities of the recombinant proteins are similar to those of Y. pseudotuberculosis native porins.
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ISSN:1068-1620
1608-330X
DOI:10.1007/s11171-008-2004-0