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Structural Basis of Glycogen Biosynthesis Regulation in Bacteria

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Author(s)

  • Javier O Cifuente
  • Natalia Comino
  • Julene Madariaga-Marcos
  • Sonia López-Fernández
  • Mikel García-Alija
  • Jon Agirre
  • David Albesa-Jové
  • Marcelo E Guerin

Department/unit(s)

Publication details

JournalStructure
DateAccepted/In press - 30 Jun 2016
DateE-pub ahead of print - 18 Aug 2016
DatePublished (current) - 6 Sep 2016
Issue number9
Volume24
Number of pages10
Pages (from-to)1613-1622
Early online date18/08/16
Original languageEnglish

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.

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© 2016 Elsevier Ltd. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

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