Characterization of the nucleoside-binding site inside the Tsx channel of Escherichia coli outer membrane Reconstitution experiments with lipid bilayer membranes

1988 ◽  
Vol 176 (3) ◽  
pp. 699-705 ◽  
Author(s):  
Roland BENZ ◽  
Angela SCHMID ◽  
Christl MAIER ◽  
Erhard BREMER
1995 ◽  
Vol 105 (3) ◽  
pp. 385-401 ◽  
Author(s):  
C Andersen ◽  
M Jordy ◽  
R Benz

LamB (maltoporin) of Escherichia coli outer membrane was reconstituted into artificial lipid bilayer membranes. The channel contains a binding site for sugars and is blocked for ions when the site is occupied by a sugar. The on and off reactions of sugar binding cause an increase of the noise of the current through the channel. The sugar-induced current noise of maltoporin was used for the evaluation of the sugar-binding kinetics for different sugars of the maltooligosaccharide series and for sucrose. The on rate constant for sugar binding was between 10(6) and 10(7) M-1.s-1 for the maltooligosaccharides and corresponds to the movement of the sugars from the aqueous phase to the central binding site. The off rate (corresponding to the release of the sugars from the channel) decreased with increasing number of glucose residues in the maltooligosaccharides from approximately 2,000 s-1 for maltotriose to 180 s-1 for maltoheptaose. The kinetics for sucrose movement was considerably slower. The activation energies of the stability constant and of the rate constants for sugar binding were evaluated from noise experiments at different temperatures. The role of LamB in the transport of maltooligosaccharides across the outer membrane is discussed.


2009 ◽  
Vol 106 (51) ◽  
pp. 21990-21995 ◽  
Author(s):  
E. Udho ◽  
K. S. Jakes ◽  
S. K. Buchanan ◽  
K. J. James ◽  
X. Jiang ◽  
...  

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