1m6j

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[[Image:1m6j.jpg|left|200px]]<br /><applet load="1m6j" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m6j, resolution 1.50&Aring;" />
 
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'''CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA==
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Triosephosphate isomerase (TIM) has been proposed as a target for drug design. TIMs from several parasites have a cysteine residue at the dimer interface, whose derivatization with thiol-specific reagents induces enzyme inactivation and aggregation. TIMs lacking this residue, such as human TIM, are less affected. TIM from Entamoeba histolytica (EhTIM) has the interface cysteine residue and presents more than ten insertions when compared with the enzyme from other pathogens. To gain further insight into the role that interface residues play in the stability and reactivity of these enzymes, we determined the high-resolution structure and characterized the effect of methylmethane thiosulfonate (MMTS) on the activity and conformational properties of EhTIM. The structure of this enzyme was determined at 1.5A resolution using molecular replacement, observing that the dimer is not symmetric. EhTIM is completely inactivated by MMTS, and dissociated into stable monomers that possess considerable secondary structure. Structural and spectroscopic analysis of EhTIM and comparison with TIMs from other pathogens reveal that conformational rearrangements of the interface after dissociation, as well as intramonomeric contacts formed by the inserted residues, may contribute to the unusual stability of the derivatized EhTIM monomer.
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<StructureSection load='1m6j' size='340' side='right'caption='[[1m6j]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M6J 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]] 1.5&#8491;</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=1m6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6j OCA], [https://pdbe.org/1m6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6j RCSB], [https://www.ebi.ac.uk/pdbsum/1m6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_ENTHI TPIS_ENTHI]
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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/m6/1m6j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1m6j ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6J OCA].
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*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica., Rodriguez-Romero A, Hernandez-Santoyo A, del Pozo Yauner L, Kornhauser A, Fernandez-Velasco DA, J Mol Biol. 2002 Sep 27;322(4):669-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12270704 12270704]
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[[Category: Entamoeba histolytica]]
[[Category: Entamoeba histolytica]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Triose-phosphate isomerase]]
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[[Category: Fernandez-Velasco DA]]
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[[Category: Fernandez-Velasco, D A.]]
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[[Category: Hernandez-Santoyo A]]
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[[Category: Hernandez-Santoyo, A.]]
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[[Category: Rodriguez-Romero A]]
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[[Category: Rodriguez-Romero, A.]]
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[[Category: asymmetry]]
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[[Category: entamoeba histolytica]]
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[[Category: monomer stability]]
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[[Category: triosephosphate isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:03 2008''
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Current revision

CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA

PDB ID 1m6j

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