5L6S

Crystal structure of E. coli ADP-glucose pyrophosphorylase (AGPase) in complex with a positive allosteric regulator beta-fructose-1,6-diphosphate (FBP) - AGPase*FBP

5L6S の概要

• エントリーDOI: 10.2210/pdb5l6s/pdb
• 分子名称: Glucose-1-phosphate adenylyltransferase, SULFATE ION, 1,6-di-O-phosphono-beta-D-fructofuranose (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 785244.36

構造登録者

Cifuente, J.O.,Albesa-Jove, D.,Comino, N.,Madariaga-Marcos, J.,Agirre, J.,Lopez-Fernandez, S.,Garcia-Alija, M.,Guerin, M.E. (登録日: 2016-05-31, 公開日: 2016-09-07, 最終更新日: 2024-01-10)

主引用文献

Cifuente, J.O.,Comino, N.,Madariaga-Marcos, J.,Lopez-Fernandez, S.,Garcia-Alija, M.,Agirre, J.,Albesa-Jove, D.,Guerin, M.E.
Structural Basis of Glycogen Biosynthesis Regulation in Bacteria.
Structure, 24:1613-1622, 2016

PubMed Abstract: ADP-glucose pyrophosphorylase (AGPase) catalyzes the rate-limiting step of bacterial glycogen and plant starch biosynthesis, the most common carbon storage polysaccharides in nature. A major challenge is to understand how AGPase activity is regulated by metabolites in the energetic flux within the cell. Here we report crystal structures of the homotetrameric AGPase from Escherichia coli in complex with its physiological positive and negative allosteric regulators, fructose-1,6-bisphosphate (FBP) and AMP, and sucrose in the active site. FBP and AMP bind to partially overlapping sites located in a deep cleft between glycosyltransferase A-like and left-handed β helix domains of neighboring protomers, accounting for the fact that sensitivity to inhibition by AMP is modulated by the concentration of the activator FBP. We propose a model in which the energy reporters regulate EcAGPase catalytic activity by intra-protomer interactions and inter-protomer crosstalk, with a sensory motif and two regulatory loops playing a prominent role.

PubMed: 27545622
DOI: 10.1016/j.str.2016.06.023

実験手法

X-RAY DIFFRACTION (3.04 Å)