6P0Y

Cryptosporidium parvum pyruvate kinase in complex with ADP

6P0Y の概要

• エントリーDOI: 10.2210/pdb6p0y/pdb
• 関連するPDBエントリー: 4DRS
• 分子名称: Pyruvate kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: pyruvate, kinase, glycolysis, cryptosporidium, transferase, allosteric enzyme
• 由来する生物種: Cryptosporidium parvum (strain Iowa II)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114032.48

構造登録者

Schormann, N.,Chattopadhyay, D. (登録日: 2019-05-17, 公開日: 2019-08-21, 最終更新日: 2024-11-20)

主引用文献

Schormann, N.,Hayden, K.L.,Lee, P.,Banerjee, S.,Chattopadhyay, D.
An overview of structure, function, and regulation of pyruvate kinases.
Protein Sci., 28:1771-1784, 2019

PubMed Abstract: In the last step of glycolysis Pyruvate kinase catalyzes the irreversible conversion of ADP and phosphoenolpyruvate to ATP and pyruvic acid, both crucial for cellular metabolism. Thus pyruvate kinase plays a key role in controlling the metabolic flux and ATP production. The hallmark of the activity of different pyruvate kinases is their tight modulation by a variety of mechanisms including the use of a large number of physiological allosteric effectors in addition to their homotropic regulation by phosphoenolpyruvate. Binding of effectors signals precise and orchestrated movements in selected areas of the protein structure that alter the catalytic action of these evolutionarily conserved enzymes with remarkably conserved architecture and sequences. While the diverse nature of the allosteric effectors has been discussed in the literature, the structural basis of their regulatory effects is still not well understood because of the lack of data representing conformations in various activation states. Results of recent studies on pyruvate kinases of different families suggest that members of evolutionarily related families follow somewhat conserved allosteric strategies but evolutionarily distant members adopt different strategies. Here we review the structure and allosteric properties of pyruvate kinases of different families for which structural data are available.

PubMed: 31342570
DOI: 10.1002/pro.3691

実験手法

X-RAY DIFFRACTION (2.6 Å)