3ODM

Archaeal-type phosphoenolpyruvate carboxylase

3ODM の概要

• エントリーDOI: 10.2210/pdb3odm/pdb
• 分子名称: Phosphoenolpyruvate carboxylase, GOLD (I) CYANIDE ION, MALONATE ION, ... (4 entities in total)
• 機能のキーワード: beta-barrel, lyase
• 由来する生物種: Clostridium perfringens
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 516277.86

構造登録者

Dunten, P.W. (登録日: 2010-08-11, 公開日: 2011-02-02, 最終更新日: 2024-02-21)

主引用文献

Dharmarajan, L.,Kraszewski, J.L.,Mukhopadhyay, B.,Dunten, P.W.
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.
Proteins, 79:1820-1829, 2011

PubMed Abstract: The crystal structure of an archaeal-type phosphoenolpyruvate carboxylase from Clostridium perfringens has been determined based on X-ray data extending to 3 Å. The asymmetric unit of the structure includes two tetramers (each a dimer-of-dimers) of the enzyme. The precipitant, malonate, employed for the crystallization is itself a weak inhibitor of phosphoenolpyruvate carboxylase and a malonate molecule is seen in the active-site in the crystal structure. The allosteric binding sites for aspartate (an inhibitor) and glucose-6-phosphate (an activator) observed in the Escherichia coli and Zea mays phosphoenolpyruvate carboxylase structures, respectively, are not conserved in the C. perfringens structure. Aspartate inhibits the C. perfringens enzyme competitively with respect to the substrate, Mg(++.) phosphoenolpyruvate. A mechanism for inhibition is proposed based on the structure and sequence comparisons with other archaeal-type phosphoenolpyruvate carboxylases with differing sensitivity to inhibition by aspartate.

PubMed: 21491491
DOI: 10.1002/prot.23006

実験手法

X-RAY DIFFRACTION (2.95 Å)