The allosteric control mechanism of bacterial glycogen biosynthesis disclosed by cryoEM.

AGPase, ADP-glucose pyrophosphorylase AMP, adenosine 5′-monophosphate ATP, adenosine 5′-triphosphate EcAGPase, AGPase from E. coli Enzyme allosterism FBP, fructose 1,6-bisphosphate G1P, α-d-glucose-1-phosphate GBE, glycogen branching enzyme GDE, glycogen debranching enzyme GP, glycogen phosphorylase GS, glycogen synthase GTA-like, glycosyltransferase-A like domain Glycogen biosynthesis Glycogen regulation LβH, left-handed β-helix domain Nucleotide sugar biosynthesis PPi, pyrophosphate RIN, residue interaction network SM, sensory motif

Journal

Current research in structural biology
ISSN: 2665-928X
Titre abrégé: Curr Res Struct Biol
Pays: Netherlands
ID NLM: 101767537

Informations de publication

Date de publication:
2020
Historique:
received: 12 02 2020
revised: 12 04 2020
accepted: 20 04 2020
entrez: 8 7 2021
pubmed: 1 5 2020
medline: 1 5 2020
Statut: epublish

Résumé

Glycogen and starch are the major carbon and energy reserve polysaccharides in nature, providing living organisms with a survival advantage. The evolution of the enzymatic machinery responsible for the biosynthesis and degradation of such polysaccharides, led the development of mechanisms to control the assembly and disassembly rate, to store and recover glucose according to cell energy demands. The tetrameric enzyme ADP-glucose pyrophosphorylase (AGPase) catalyzes and regulates the initial step in the biosynthesis of both α-polyglucans. AGPase displays cooperativity and allosteric regulation by sensing metabolites from the cell energy flux. The understanding of the allosteric signal transduction mechanisms in AGPase arises as a long-standing challenge. In this work, we disclose the cryoEM structures of the paradigmatic homotetrameric AGPase from

Identifiants

pubmed: 34235472
doi: 10.1016/j.crstbi.2020.04.005
pii: S2665-928X(20)30009-X
pmc: PMC8244506
doi:

Types de publication

Journal Article

Langues

eng

Pagination

89-103

Informations de copyright

© 2020 The Author(s).

Déclaration de conflit d'intérêts

The authors declare no financial conflict of interest.

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Auteurs

Javier O Cifuente (JO)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

Natalia Comino (N)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

Cecilia D'Angelo (C)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

Alberto Marina (A)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

David Gil-Carton (D)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

David Albesa-Jové (D)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.

Marcelo E Guerin (ME)

Structural Biology Unit, CIC BioGUNE, Bizkaia Technology Park, 48160, Derio, Spain.
IKERBASQUE, Basque Foundation for Science, 48013, Bilbao, Spain.

Classifications MeSH