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Structural Basis of Glycogen Biosynthesis Regulation in Bacteria

DOI: 10.1016/j.str.2016.06.023 DOI Help

Authors: Javier O. Cifuente (Structural Biology Unit, CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU);) , Natalia Comino (Structural Biology Unit, CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU);) , Julene Madariaga-marcos (Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU)) , Sonia López-fernández (Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU)) , Mikel García-alija (Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU)) , Jon Agirre (The University of York) , David Albesa-jove (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU); IKERBASQUE) , Marcelo E. Guerin (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU); IKERBASQUE)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 24 , PAGES 1613 - 1622

State: Published (Approved)
Published: September 2016
Diamond Proposal Number(s): 10130 , 8302

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.

Journal Keywords: ADP-glucose pyrophosphorylase, glycogen, regulation

Subject Areas: Biology and Bio-materials, Chemistry, Energy


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Other Facilities: SOLEIL