Replacement of the Sole Histidinyl Residue in OmpF Porin fromE. coliby Threonine (H21T) Does Not Affect Channel Structure and Function

The sole histidine residue in OmpF porin was replaced by threonine using site-directed mutagenesis. This exchange affected neither channel properties nor channel structure, as determined by X-ray analysis to 3.2 Å. Conductance and critical voltage (Vc) were observed in the pH range 4.3–9.4, with res...

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Published in:Biochemical and biophysical research communications 1996-06, Vol.223 (1), p.118-122
Main Authors: Saint, Nathalie, Prilipov, Alexej, Hardmeyer, Ariane, Lou, Kuo-Long, Schirmer, Tilman, Rosenbusch, Jurg P.
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container_title Biochemical and biophysical research communications
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creator Saint, Nathalie
Prilipov, Alexej
Hardmeyer, Ariane
Lou, Kuo-Long
Schirmer, Tilman
Rosenbusch, Jurg P.
description The sole histidine residue in OmpF porin was replaced by threonine using site-directed mutagenesis. This exchange affected neither channel properties nor channel structure, as determined by X-ray analysis to 3.2 Å. Conductance and critical voltage (Vc) were observed in the pH range 4.3–9.4, with results indistinguishable from those observed in the wild-type protein. The validity of these observations is supported by the independence of the methods used, and by the fact that mutants in residues located in the channel constriction yielded significantly different values from wild-type protein. The binding of a glycolipid molecule might be affected.
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title Replacement of the Sole Histidinyl Residue in OmpF Porin fromE. coliby Threonine (H21T) Does Not Affect Channel Structure and Function
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