Structure analysis of Entamoeba histolytica enolase

Eike C. Schulz, Michael Tietzel, Ayala Tovy, Serge Ankri, Ralf Ficner

Research output: Contribution to journalArticlepeer-review

Abstract

Entamoeba histolytica enolase (EhENO) reversibly inter-converts 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.

Original languageEnglish
Pages (from-to)619-627
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume67
Issue number7
DOIs
StatePublished - Jul 2011

Keywords

  • Entamoeba histolytica
  • enolase
  • glycolysis

All Science Journal Classification (ASJC) codes

  • Structural Biology

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