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1lta
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==2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE== | ==2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE== | ||
| - | <StructureSection load='1lta' size='340' side='right' caption='[[1lta]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1lta' size='340' side='right'caption='[[1lta]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lta]] is a 7 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1lta]] is a 7 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=1LTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTA FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>< | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> |
| - | <table> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lta OCA], [https://pdbe.org/1lta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lta RCSB], [https://www.ebi.ac.uk/pdbsum/1lta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lta 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lta_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lta_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1lta ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex. | ||
| - | |||
| - | Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT).,Merritt EA, Sixma TK, Kalk KH, van Zanten BA, Hol WG Mol Microbiol. 1994 Aug;13(4):745-53. PMID:7997185<ref>PMID:7997185</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Hol WGJ]] |
| - | [[Category: | + | [[Category: Kalk KH]] |
| - | [[Category: | + | [[Category: Merritt EA]] |
| - | [[Category: | + | [[Category: Sixma TK]] |
| - | [[Category: | + | [[Category: Van Zanten BAM]] |
Current revision
2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE
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