The hinge portion of the S. aureus alpha-toxin crosses the lipid bilayer and is part of the trans-mouth of the channel.
Biochim Biophys Acta
; 1329(1): 51-60, 1997 Oct 02.
Article
in En
| MEDLINE
| ID: mdl-9370244
ABSTRACT
This paper compares the functional properties of ion channels formed in planar lipid membranes by the wild and mutant Staphylococcus aureus alpha-toxin. It was shown that replacement of the amino acid Gly at position 130 by Cys in the primary structure of the toxin decreases the single-channel conductance with a concomitant decrease in the pH at which the channel becomes unable to discriminate between Cl- and K+ ions. The mutation also induced an increase in the asymmetry in the current-voltage relationship of the channel. The results of our experiments suggest that the trans-mouth of the channel is responsible for all the observed changes in channel properties. It was assumed that this entrance is built by the glycine-rich hinge portion of the toxin and is situated close to the surface of monolayer facing the trans-compartment.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Staphylococcus aureus
/
Bacterial Toxins
/
Hemolysin Proteins
/
Ion Channels
/
Lipid Bilayers
Language:
En
Journal:
Biochim Biophys Acta
Year:
1997
Document type:
Article
Affiliation country:
Uzbekistan