3QTP

Crystal Structure Analysis of Entamoeba histolytica Enolase

3QTP の概要

• エントリーDOI: 10.2210/pdb3qtp/pdb
• 分子名称: Enolase 1, 2-PHOSPHOGLYCERIC ACID, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: glycolysis, enolase, lyase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96590.23

構造登録者

Schulz, E.C.,Ficner, R. (登録日: 2011-02-23, 公開日: 2011-07-13, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)