1lt3

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[[Image:1lt3.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1lt3| PDB=1lt3 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt3 OCA], [http://www.ebi.ac.uk/pdbsum/1lt3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lt3 RCSB]</span>
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'''HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C'''
'''HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C'''
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[[Category: Akker, F Van Den.]]
[[Category: Akker, F Van Den.]]
[[Category: Hol, W G.J.]]
[[Category: Hol, W G.J.]]
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[[Category: enterotoxin]]
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[[Category: Enterotoxin]]
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[[Category: signal]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:15:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:02 2008''
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Revision as of 21:15, 2 May 2008

Image:1lt3.jpg

Template:STRUCTURE 1lt3

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 Page seeded by OCA on Sat May 3 00:15:39 2008

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