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[[Image:3qtp.jpg|left|200px]]


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==Crystal Structure Analysis of Entamoeba histolytica Enolase==
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<StructureSection load='3qtp' size='340' side='right'caption='[[3qtp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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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]] 1.9&#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=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_3qtp|  PDB=3qtp  |  SCENE=  }}
<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>
</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;">
== 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.


===Crystal Structure Analysis of Entamoeba histolytica Enolase===
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<ref>PMID:21697600</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qtp" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Enolase 3D structures|Enolase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 21697600 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21697600}}
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</StructureSection>
==About this Structure==
[[3qtp]] is a 2 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:021697600</ref><references group="xtra"/>
[[Category: Entamoeba histolytica]]
[[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]]

Latest revision as of 12:37, 30 October 2024

Crystal Structure Analysis of Entamoeba histolytica EnolaseCrystal Structure Analysis of Entamoeba histolytica Enolase

Structural highlights

3qtp is a 2 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

3qtp, resolution 1.90Å

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