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| | ==Crystal Structure Analysis of Entamoeba histolytica Enolase== | | ==Crystal Structure Analysis of Entamoeba histolytica Enolase== |
| - | <StructureSection load='3qtp' size='340' side='right' caption='[[3qtp]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3qtp' size='340' side='right'caption='[[3qtp]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qtp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QTP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qtp]] 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=3QTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QTP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ENL-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qtp OCA], [https://pdbe.org/3qtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qtp RCSB], [https://www.ebi.ac.uk/pdbsum/3qtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qtp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qtp OCA], [http://pdbe.org/3qtp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qtp RCSB], [http://www.ebi.ac.uk/pdbsum/3qtp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qtp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ENO_ENTH1 ENO_ENTH1] Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:15794763). Inhibits tRNA methyltransferase METH catalytic activity in the absence of 2-phosphoglycerate (PubMed:20174608).<ref>PMID:15794763</ref> <ref>PMID:20174608</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Enolase|Enolase]] | + | *[[Enolase 3D structures|Enolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enthi]] | + | [[Category: Entamoeba histolytica]] |
| - | [[Category: Phosphopyruvate hydratase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ficner, R]] | + | [[Category: Ficner R]] |
| - | [[Category: Schulz, E C]] | + | [[Category: Schulz EC]] |
| - | [[Category: Enolase]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
ENO_ENTH1 Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:15794763). Inhibits tRNA methyltransferase METH catalytic activity in the absence of 2-phosphoglycerate (PubMed:20174608).[1] [2]
Publication Abstract from PubMed
Entamoeba histolytica enolase (EhENO) reversibly interconverts 2-phosphoglyceric acid (2-PGA) and phosphoenolpyruvic acid (PEP). The crystal structure of the homodimeric EhENO is presented at a resolution of 1.9 A. In the crystal structure EhENO presents as an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation. Interestingly, both active sites contain a copurified 2-PGA molecule. While the 2-PGA molecule in the closed active site closely resembles the conformation known from other enolase-2-PGA complexes, the conformation in the open active site is different. Here, 2-PGA is shifted approximately 1.6 A away from metal ion I, most likely representing a precatalytic situation.
Structure analysis of Entamoeba histolytica enolase.,Schulz EC, Tietzel M, Tovy A, Ankri S, Ficner R Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):619-27. Epub 2011, Jun 14. PMID:21697600[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saavedra E, Encalada R, Pineda E, Jasso-Chávez R, Moreno-Sánchez R. Glycolysis in Entamoeba histolytica. Biochemical characterization of recombinant glycolytic enzymes and flux control analysis. FEBS J. 2005 Apr;272(7):1767-83. PMID:15794763 doi:10.1111/j.1742-4658.2005.04610.x
- ↑ Tovy A, Siman Tov R, Gaentzsch R, Helm M, Ankri S. A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity. PLoS Pathog. 2010 Feb 19;6(2):e1000775. PMID:20174608 doi:10.1371/journal.ppat.1000775
- ↑ Schulz EC, Tietzel M, Tovy A, Ankri S, Ficner R. Structure analysis of Entamoeba histolytica enolase. Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):619-27. Epub 2011, Jun 14. PMID:21697600 doi:10.1107/S0907444911016544
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