title: Structure analysis of Entamoeba histolytica enolase.
abstract: 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 Å. 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 Å away from metal ion I, most likely representing a precatalytic situation.
authors.affiliation: Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig Weg, Germany. eschulz1@gwdg.de
authors.forename: Eike C
authors.initials: EC
authors.lastname: Schulz
authors.forename: Michael
authors.initials: M
authors.lastname: Tietzel
authors.forename: Ayala
authors.initials: A
authors.lastname: Tovy
authors.forename: Serge
authors.initials: S
authors.lastname: Ankri
authors.forename: Ralf
authors.initials: R
authors.lastname: Ficner
mesh_terms: D018360:Crystallography, X-Ray; D004748:Entamoeba histolytica / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D010751:Phosphopyruvate Hydratase