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1ltt

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Revision as of 08:01, 11 September 2015

LACTOSE BINDING TO HEAT-LABILE ENTEROTOXIN REVEALED BY X-RAY CRYSTALLOGRAPHY

Structural highlights

1ltt is a 7 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The September 2005 RCSB PDB Molecule of the Month feature on Cholera Toxin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [ELAP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Recognition of the oligosaccharide portion of ganglioside GM1 in membranes of target cells by the heat-labile enterotoxin from Escherichia coli is the crucial first step in its pathogenesis, as it is for the closely related cholera toxin. These toxins have five B subunits, which are essential for GM1 binding, and a single A subunit, which needs to be nicked by proteolysis and reduced, yielding an A1-'enzyme' and an A2-'linker' peptide. A1 is translocated across the membrane of intestinal epithelial cells, possibly after endocytosis, upon which it ADP-ribosylates the G protein Gs alpha. The mechanism of binding and translocation of these toxins has been extensively investigated, but how the protein is orientated on binding is still not clear. Knowing the precise arrangement of the ganglioside binding sites of the toxins will be useful for designing drugs against the diarrhoeal diseases caused by organisms secreting these toxins and in the development of oral vaccines against them. We present here the three-dimensional structure of the E. coli heat-labile enterotoxin complexed with lactose. This reveals the location of the binding site of the terminal galactose of GM1, which is consistent with toxin binding to the target cell with its A1 fragment pointing away from the membrane. A small helix is identified at the carboxy terminus of A2 which emerges through the central pore of the B subunits and probably comes into contact with the membrane upon binding, whereas the A1 subunit is flexible with respect to the B pentamer.

Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography.,Sixma TK, Pronk SE, Kalk KH, van Zanten BA, Berghuis AM, Hol WG Nature. 1992 Feb 6;355(6360):561-4. PMID:1741035^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sixma TK, Pronk SE, Kalk KH, van Zanten BA, Berghuis AM, Hol WG. Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature. 1992 Feb 6;355(6360):561-4. PMID:1741035 doi:http://dx.doi.org/10.1038/355561a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ltt"

@@ Line 2: / Line 2: @@
 <StructureSection load='1ltt' size='340' side='right' caption='[[1ltt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ltt]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The September 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cholera Toxin''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_9 10.2210/rcsb_pdb/mom_2005_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LTT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ltt]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The September 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cholera Toxin''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_9 10.2210/rcsb_pdb/mom_2005_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LTT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ltt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ltt RCSB], [http://www.ebi.ac.uk/pdbsum/1ltt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ltt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ltt OCA], [http://pdbe.org/1ltt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ltt RCSB], [http://www.ebi.ac.uk/pdbsum/1ltt PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ELBP_ECOLI ELBP_ECOLI]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [[http://www.uniprot.org/uniprot/ELAP_ECOLI ELAP_ECOLI]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
+[[http://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. [[http://www.uniprot.org/uniprot/ELAP_ECOLX ELAP_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]]
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ltt" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Bacillus coli migula 1895]]
 [[Category: Cholera Toxin]]
-[[Category: Escherichia coli]]
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: Hol, W G.J]]
 [[Category: Sixma, T K]]
 [[Category: Toxin]]

1ltt

From Proteopedia

Revision as of 08:01, 11 September 2015

LACTOSE BINDING TO HEAT-LABILE ENTEROTOXIN REVEALED BY X-RAY CRYSTALLOGRAPHY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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