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

Summary for 5L6S

• Entry DOI: 10.2210/pdb5l6s/pdb
• Descriptor: Glucose-1-phosphate adenylyltransferase, SULFATE ION, 1,6-di-O-phosphono-beta-D-fructofuranose (3 entities in total)
• Functional Keywords: transferase
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 16
• Total formula weight: 785244.36

Authors

Cifuente, J.O.,Albesa-Jove, D.,Comino, N.,Madariaga-Marcos, J.,Agirre, J.,Lopez-Fernandez, S.,Garcia-Alija, M.,Guerin, M.E. (deposition date: 2016-05-31, release date: 2016-09-07, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.04 Å)