3ODM

Archaeal-type phosphoenolpyruvate carboxylase

Summary for 3ODM

• Entry DOI: 10.2210/pdb3odm/pdb
• Descriptor: Phosphoenolpyruvate carboxylase, GOLD (I) CYANIDE ION, MALONATE ION, ... (4 entities in total)
• Functional Keywords: beta-barrel, lyase
• Biological source: Clostridium perfringens
• Total number of polymer chains: 8
• Total formula weight: 516277.86

Authors

Dunten, P.W. (deposition date: 2010-08-11, release date: 2011-02-02, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.95 Å)