1lta

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(New page: 200px<br /><applet load="1lta" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lta, resolution 2.2&Aring;" /> '''2.2 ANGSTROMS CRYSTAL...)
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[[Image:1lta.jpg|left|200px]]<br /><applet load="1lta" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lta, resolution 2.2&Aring;" />
 
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'''2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE'''<br />
 
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==Overview==
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==2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE==
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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.
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<StructureSection load='1lta' size='340' side='right'caption='[[1lta]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lta_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1LTA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GAL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7997185 7997185]
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</div>
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<div class="pdbe-citations 1lta" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hol WGJ]]
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[[Category: Kalk, K.H.]]
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[[Category: Kalk KH]]
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[[Category: Merritt, E.A.]]
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[[Category: Merritt EA]]
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[[Category: Sixma, T.K.]]
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[[Category: Sixma TK]]
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[[Category: Zanten, B.A.M.Van.]]
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[[Category: Van Zanten BAM]]
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[[Category: GAL]]
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[[Category: enterotoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:51:49 2007''
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2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE

PDB ID 1lta

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