[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 were selected for isolation and refolding of recombinant monomer and porin trimer. Their spatial structures were characterized by the intrinsic protein fluorescence and CD spectroscopy. It was shown that the recombinant porins are similar in the composition of secondary structure elements to the 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. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2008, vol. 34, no. 2; see also http://www.maik.ru.
Khomenko
V A
VA
Portniagina
O Iu
OIu
Novikova
O D
OD
Isaeva
M P
MP
Kim
N Iu
NIu
Likhatskaia
G N
GN
Vostrikova
O P
OP
Solov'eva
T F
TF
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D002462:Cell Membrane / Q000737:chemistry; D002942:Circular Dichroism; D005453:Fluorescence; D007118:Immunoassay; D008051:Lipid Bilayers / Q000737:chemistry; D018272:Porins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D015011:Yersinia pseudotuberculosis / Q000166:cytology*
D001425:Bacterial Outer Membrane Proteins; D008051:Lipid Bilayers; C109237:OmpF protein; D018272:Porins; D011994:Recombinant Proteins