1lt3

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{{STRUCTURE_1lt3| PDB=1lt3 | SCENE= }}
{{STRUCTURE_1lt3| PDB=1lt3 | SCENE= }}
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'''HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C'''
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===HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9416616 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9416616}}
==About this Structure==
==About this Structure==
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[[Category: Enterotoxin]]
[[Category: Enterotoxin]]
[[Category: Signal]]
[[Category: Signal]]
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Revision as of 19:07, 2 July 2008

Template:STRUCTURE 1lt3

HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C

Template:ABSTRACT PUBMED 9416616

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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