1qnu: Difference between revisions

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-{{Seed}}
-[[Image:1qnu.png|left|200px]]
-<!--
+==Shiga-Like Toxin I B Subunit Complexed with the Bridged-Starfish Inhibitor==
-The line below this paragraph, containing "STRUCTURE_1qnu", creates the "Structure Box" on the page.
+<StructureSection load='1qnu' size='340' side='right'caption='[[1qnu]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1qnu]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNU FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMB:METHYL-CARBAMIC+ACID+ETHYL+ESTER'>EMB</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MEC:ETHYL-CARBAMIC+ACID+METHYL+ESTER'>MEC</scene></td></tr>
-{{STRUCTURE_1qnu|  PDB=1qnu  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qnu OCA], [https://pdbe.org/1qnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qnu RCSB], [https://www.ebi.ac.uk/pdbsum/1qnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qnu ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/V5URS0_9CAUD V5URS0_9CAUD] The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.[ARBA:ARBA00003218]
+== 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/qn/1qnu_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=1qnu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The diseases caused by Shiga and cholera toxins account for the loss of millions of lives each year. Both belong to the clinically significant subset of bacterial AB5 toxins consisting of an enzymatically active A subunit that gains entry to susceptible mammalian cells after oligosaccharide recognition by the B5 homopentamer. Therapies might target the obligatory oligosaccharide-toxin recognition event, but the low intrinsic affinity of carbohydrate-protein interactions hampers the development of low-molecular-weight inhibitors. The toxins circumvent low affinity by binding simultaneously to five or more cell-surface carbohydrates. Here we demonstrate the use of the crystal structure of the B5 subunit of Escherichia coli O157:H7 Shiga-like toxin I (SLT-I) in complex with an analogue of its carbohydrate receptor to design an oligovalent, water-soluble carbohydrate ligand (named STARFISH), with subnanomolar inhibitory activity. The in vitro inhibitory activity is 1-10-million-fold higher than that of univalent ligands and is by far the highest molar activity of any inhibitor yet reported for Shiga-like toxins I and II. Crystallography of the STARFISH/Shiga-like toxin I complex explains this activity. Two trisaccharide receptors at the tips of each of five spacer arms simultaneously engage all five B subunits of two toxin molecules.
-===SHIGA-LIKE TOXIN I B SUBUNIT COMPLEXED WITH THE BRIDGED-STARFISH INHIBITOR===
+Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands.,Kitov PI, Sadowska JM, Mulvey G, Armstrong GD, Ling H, Pannu NS, Read RJ, Bundle DR Nature. 2000 Feb 10;403(6770):669-72. PMID:10688205<ref>PMID:10688205</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qnu" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10688205}}, adds the Publication Abstract to the page
+*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10688205 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10688205}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli O157:H7]]
-QNU is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_h30,_bacteriophaurce_3 Bacteriophage h30, bacteriophaurce 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNU OCA].
+[[Category: Large Structures]]
+[[Category: Hayakawa K]]
-==Reference==
+[[Category: Pannu NS]]
-<ref group="xtra">PMID:10688205</ref><references group="xtra"/>
+[[Category: Read RJ]]
-[[Category: Bacteriophage h30, bacteriophaurce 3]]
-[[Category: Hayakawa, K.]]
-[[Category: Pannu, N S.]]
-[[Category: Read, R J.]]
-[[Category: Multivalent protein-carbohydrate recognition]]
-[[Category: Ob-fold]]
-[[Category: Subnanomolar inhibitor]]
-[[Category: Toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:47:44 2009''