1ZXX

The crystal structure of phosphofructokinase from Lactobacillus delbrueckii

1ZXX の概要

• エントリーDOI: 10.2210/pdb1zxx/pdb
• 分子名称: 6-phosphofructokinase, SULFATE ION (3 entities in total)
• 機能のキーワード: phosphofructokinase, allosteric regulation, lactobacillus bulgaricus, transferase
• 由来する生物種: Lactobacillus delbrueckii subsp. bulgaricus
• 細胞内の位置: Cytoplasm: P80019
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34240.59

構造登録者

Paricharttanakul, N.M.,Ye, S.,Menefee, A.L.,Javid-Majd, F.,Sacchettini, J.C.,Reinhart, G.D. (登録日: 2005-06-09, 公開日: 2005-11-08, 最終更新日: 2024-02-14)

主引用文献

Paricharttanakul, N.M.,Ye, S.,Menefee, A.L.,Javid-Majd, F.,Sacchettini, J.C.,Reinhart, G.D.
Kinetic and Structural Characterization of Phosphofructokinase from Lactobacillus bulgaricus.
Biochemistry, 44:15280-15286, 2005

PubMed Abstract: Phosphofructokinase from Lactobacillus delbrueckii subspecies bulgaricus (LbPFK) has been reported to be a nonallosteric analogue of phosphofructokinase from Escherichia coli at pH 8.2 [Le Bras et al. (1991) Eur. J. Biochem. 198, 683-687]. A reexamination of the kinetics of this enzyme shows LbPFK to have limited binding affinity toward the allosteric ligands, MgADP and PEP, with dissociation constants of approximately 20 mM for both. Their allosteric effects are observed only at high concentrations of these ligands, with both exhibiting inhibitory effects on substrate binding. No pH dependence was observed for the binding and the influence of MgADP and PEP on the enzyme. To attempt to explain these results, the crystal structure of LbPFK was solved using molecular replacement to 1.86 A resolution. A comparative study of the LbPFK structure with that of phosphofructokinases from E. coli (EcPFK) and Bacillus stearothermophilus (BsPFK) reveals a structure with conserved fold and substrate binding site. The effector binding site, however, shows many differences that could explain the observed decreases in binding affinity for MgADP and PEP in LbPFK as compared to the other two enzymes.

PubMed: 16285731
DOI: 10.1021/bi051283g

実験手法

X-RAY DIFFRACTION (1.85 Å)