3QTP

Crystal Structure Analysis of Entamoeba histolytica Enolase

Summary for 3QTP

• Entry DOI: 10.2210/pdb3qtp/pdb
• Descriptor: Enolase 1, 2-PHOSPHOGLYCERIC ACID, SULFATE ION, ... (5 entities in total)
• Functional Keywords: glycolysis, enolase, lyase
• Biological source: Entamoeba histolytica
• Total number of polymer chains: 2
• Total formula weight: 96590.23

Authors

Schulz, E.C.,Ficner, R. (deposition date: 2011-02-23, release date: 2011-07-13, Last modification date: 2024-10-30)

Primary citation

Schulz, E.C.,Tietzel, M.,Tovy, A.,Ankri, S.,Ficner, R.
Structure analysis of Entamoeba histolytica enolase.
Acta Crystallogr.,Sect.D, 67:619-627, 2011

PubMed 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.

PubMed: 21697600
DOI: 10.1107/S0907444911016544

Experimental method

X-RAY DIFFRACTION (1.9 Å)