1lt3
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(New page: 200px<br /><applet load="1lt3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lt3, resolution 2.0Å" /> '''HEAT-LABILE ENTEROTOX...)
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Revision as of 18:44, 20 November 2007
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HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C
Overview
Cholera toxin (CT) produced by Vibrio cholerae and heat-labile enterotoxin, (LT-I), produced by enterotoxigenic Escherichia coli, are AB5, heterohexamers with an ADP-ribosylating A subunit and a GM1 receptor, binding B pentamer. These toxins are among the most potent mucosal, adjuvants known and, hence, are of interest both for the development of, anti-diarrheal vaccines against cholera or enterotoxigenic Escherichia, coli diarrhea and also for vaccines in general. However, the A subunits of, CT and LT-I are known to be relatively temperature sensitive. To improve, the thermostability of LT-I an additional disulfide bond was introduced in, the A1 subunit by means of the double mutation N40C and G166C. The crystal, structure of this double mutant of LT-I has been determined to 2.0 A, resolution. The protein structure of the N40C/G166C double mutant is very, similar to the native structure except for a few local shifts near the new, disulfide bond. The introduction of this additional disulfide bond, increases the thermal stability of the A subunit of LT-I by 6 degrees C., The enhancement in thermostability could make this disulfide bond variant, of LT-I of considerable interest for the design of enterotoxin-based, vaccines.
About this Structure
1LT3 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit., van den Akker F, Feil IK, Roach C, Platas AA, Merritt EA, Hol WG, Protein Sci. 1997 Dec;6(12):2644-9. PMID:9416616
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