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New page: left|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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[[Image:1lt3.jpg|left|200px]]<br /><applet load="1lt3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lt3, resolution 2.0&Aring;" />
'''HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C'''<br />


==Overview==
==HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C==
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.
<StructureSection load='1lt3' size='340' side='right'caption='[[1lt3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lt3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LT3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt3 OCA], [https://pdbe.org/1lt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lt3 RCSB], [https://www.ebi.ac.uk/pdbsum/1lt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lt3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lt3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:9416616</ref>
1LT3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LT3 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9416616 9416616]
</div>
<div class="pdbe-citations 1lt3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Akker, F.Van.Den.]]
[[Category: Hol WGJ]]
[[Category: Hol, W.G.J.]]
[[Category: Van Den Akker F]]
[[Category: enterotoxin]]
[[Category: signal]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:51:28 2007''

Latest revision as of 06:59, 30 October 2024

HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C

1lt3, resolution 2.00Å

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