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TitleStructural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein.
Journal, issue, pagesNat Commun, Year 2026
Publish dateApr 27, 2026
AuthorsValerio Di Domenico / Jorick Franceus / Leonardo Mastrella / Emma De Beul / Adrià Alcaide-Jiménez / Francisco Paredes-Martínez / Juan Carlos Villegas-Ruiz / Elena Holden / Alejandro Delgado Rey / Cecilia D'Angelo / Javier O Cifuente / Weston B Struwe / Ricardo M Biondi / Alberto Marina / Sean R Connell / Justin L P Benesch / Patricia Casino / Christophe Colleoni / Tom Desmet / Marcelo E Guerin /
PubMed AbstractProtein phosphorylation is a universal regulatory mechanism, controlling virtually all aspects of bacterial physiology and pathogenesis, yet histidine phosphorylation remains among the least ...Protein phosphorylation is a universal regulatory mechanism, controlling virtually all aspects of bacterial physiology and pathogenesis, yet histidine phosphorylation remains among the least understood. The histidine phosphocarrier protein HPr not only drives bacterial glucose transmembrane uptake through the phosphotransferase system (PTS), but also controls key enzymes for central carbon metabolism, including glycogen phosphorylase (GP). Here we report cryoEM structures of multimeric Escherichia coli GP and their complexes with HPr. The EM maps reveal an unanticipated density at H806 of GP, consistent with histidine phosphorylation within a histidine-rich pocket at the N-terminal domain. Enzymatic assays reveal that HPr transfers a phosphoryl group to the N1 position of a histidine residue in GP. Through an integrative structural, mutational and functional approach, we uncover the molecular basis of HPr- GP selectivity and define the allosteric mechanism by which HPr regulates GP. We establish histidine phosphorylation as a mechanism of GP regulation, expanding the traditional paradigm of glycogen metabolism control in bacteria.
External linksNat Commun / PubMed:42045210
MethodsEM (single particle)
Resolution2.06 - 3.1 Å
Structure data

54650

9s7v

EMDB-54650: Unliganded dimer - bacterial
PDB-9s7v: Structure of glycogen phosphorylase - dimeric form - from Escherichia coli
Method: EM (single particle) / Resolution: 3.1 Å

54651

9s86

EMDB-54651: Unliganded tetramer of Glycogen phosphorylase from E. coli
PDB-9s86: Structure of glycogen phosphorylase - tetrameric form - from Escherichia coli
Method: EM (single particle) / Resolution: 2.97 Å

54658

9s8b

EMDB-54658: Complexed dimer - bacterial
PDB-9s8b: Structure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli
Method: EM (single particle) / Resolution: 2.79 Å

54663

9s8k

EMDB-54663: Complexed tetramer - bacterial
PDB-9s8k: Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from Escherichia coli
Method: EM (single particle) / Resolution: 2.06 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Glycogen phosphorylase

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