1oep: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1oep.png|left|200px]]
-<!--
+==Structure of Trypanosoma brucei enolase reveals the inhibitory divalent metal site==
-The line below this paragraph, containing "STRUCTURE_1oep", creates the "Structure Box" on the page.
+<StructureSection load='1oep' size='340' side='right'caption='[[1oep]], [[Resolution|resolution]] 2.30&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'>[[1oep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OEP 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]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1oep|  PDB=1oep  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oep OCA], [https://pdbe.org/1oep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oep RCSB], [https://www.ebi.ac.uk/pdbsum/1oep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oep ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9NDH8_TRYBB Q9NDH8_TRYBB]
+== 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/oe/1oep_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1oep ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The glycolytic enzymes of the trypanosomatids, that cause a variety of medically and agriculturally important diseases, are validated targets for drug design. Design of species-specific inhibitors is facilitated by the availability of structural data. Irreversible inhibitors, that bound covalently to the parasite enzyme alone, would be potentially particularly effective. Here we determine the crystal structure of enolase from Trypanosoma brucei and show that two cysteine residues, located in a water-filled cavity near the active-site, are modified by iodoacetamide leading to loss of catalytic activity. Since these residues are specific to the Trypanosomatidae lineage, this finding opens the way for the development of parasite-specific, irreversibly binding enolase inhibitors. In the present structure, the catalytic site is partially occupied by sulphate and two zinc ions. Surprisingly, one of these zinc ions illustrates the existence of a novel enolase-binding site for divalent metals. Evidence suggests that this is the first direct visualization of the elusive inhibitory metal site, whose existence has hitherto only been inferred from kinetic data.
-===STRUCTURE OF TRYPANOSOMA BRUCEI ENOLASE REVEALS THE INHIBITORY DIVALENT METAL SITE===
+The crystal structure of Trypanosoma brucei enolase: visualisation of the inhibitory metal binding site III and potential as target for selective, irreversible inhibition.,da Silva Giotto MT, Hannaert V, Vertommen D, de A S Navarro MV, Rider MH, Michels PA, Garratt RC, Rigden DJ J Mol Biol. 2003 Aug 15;331(3):653-65. PMID:12899835<ref>PMID:12899835</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12899835}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1oep" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12899835 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_12899835}}
-==About this Structure==
-[[1oep]] is a 1 chain structure of [[Enolase]] with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OEP OCA].
 ==See Also==
-*[[Enolase|Enolase]]
+*[[Enolase 3D structures|Enolase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:012899835</ref><references group="xtra"/>
+__TOC__
-[[Category: Phosphopyruvate hydratase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Trypanosoma brucei brucei]]
-[[Category: Garratt, R C.]]
+[[Category: Da Silva giotto MT]]
-[[Category: Giotto, M T.Da Silva.]]
+[[Category: Garratt RC]]
-[[Category: Navarro, M V.A S.]]
+[[Category: Navarro MVAS]]
-[[Category: Rigden, D J.]]
+[[Category: Rigden DJ]]
-[[Category: Glycolysis]]
-[[Category: His-tag]]
-[[Category: Lyase]]