2OX3

R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase

2OX3 の概要

• エントリーDOI: 10.2210/pdb2ox3/pdb
• 関連するPDBエントリー: 2GQ1 2OWZ
• 分子名称: Fructose-1,6-bisphosphatase, 6-O-phosphono-beta-D-fructofuranose, PHOSPHOENOLPYRUVATE, ... (4 entities in total)
• 機能のキーワード: glycolysis, gluconeogenesis, bacteria, carbohydrate metabolism, diabetes, protein-protein interactions, proteobacteria, gram-negative, protein crystallography, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37589.41

構造登録者

Hines, J.K.,Fromm, H.J.,Honzatko, R.B. (登録日: 2007-02-19, 公開日: 2007-03-06, 最終更新日: 2024-10-30)

主引用文献

Hines, J.K.,Fromm, H.J.,Honzatko, R.B.
Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state.
J.Biol.Chem., 282:11696-11704, 2007

PubMed Abstract: The enteric bacterium Escherichia coli requires fructose-1,6-bisphosphatase (FBPase) for growth on gluconeogenic carbon sources. Constitutive expression of FBPase and fructose-6-phosphate-1-kinase coupled with the absence of futile cycling implies an undetermined mechanism of coordinate regulation involving both enzymes. Tricarboxylic acids and phosphorylated three-carbon carboxylic acids, all intermediates of glycolysis and the tricarboxylic acid cycle, are shown here to activate E. coli FBPase. The two most potent activators, phosphoenolpyruvate and citrate, bind to the sulfate anion site, revealed previously in the first crystal structure of the E. coli enzyme. Tetramers ligated with either phosphoenolpyruvate or citrate, in contrast to the sulfate-bound structure, are in the canonical R-state of porcine FBPase but nevertheless retain sterically blocked AMP pockets. At physiologically relevant concentrations, phosphoenolpyruvate and citrate stabilize an active tetramer over a less active enzyme form of mass comparable with that of a dimer. The above implies the conservation of the R-state through evolution. FBPases of heterotrophic organisms of distantly related phylogenetic groups retain residues of the allosteric activator site and in those instances where data are available exhibit activation by phosphoenolpyruvate. Findings here unify disparate observations regarding bacterial FBPases, implicating a mechanism of feed-forward activation in bacterial central metabolism.

PubMed: 17314096
DOI: 10.1074/jbc.M611104200

実験手法

X-RAY DIFFRACTION (2.18 Å)