Evidence map›Paper›PMID 42045210›Full record

ArticleNature communications2026

Structural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein.

Valerio 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 and 10 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors.

Valerio Di Domenico *Structural Glycobiology Laboratory, Department of Structural and Molecular Biology, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, Barcelona, Spain.ORCID http://orcid.org/0000-0002-8040-5854
Jorick Franceus *Centre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent, Belgium.ORCID http://orcid.org/0000-0003-4377-5933
Leonardo Mastrella *Structural Glycobiology Laboratory, Department of Structural and Molecular Biology, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, Barcelona, Spain.
Emma De BeulCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent, Belgium.
Adrià Alcaide-JiménezStructural Glycobiology Laboratory, Department of Structural and Molecular Biology, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, Barcelona, Spain.ORCID http://orcid.org/0000-0002-1015-6469
Francisco Paredes-MartínezDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Spain.
Juan Carlos Villegas-RuizStructural Glycobiology Laboratory, Department of Structural and Molecular Biology, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, Barcelona, Spain.ORCID http://orcid.org/0009-0007-3831-5285
Elena HoldenThe Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, UK.
Alejandro Delgado ReyIPICYT, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica A.C., San Luis Potosí, México.ORCID http://orcid.org/0000-0002-8869-3790
Cecilia D'AngeloStructural Glycobiology Laboratory, Biocruces Bizkaia Health Research Institute, Cruces University Hospital, 48903, Barakaldo, Bizkaia, Spain.ORCID http://orcid.org/0000-0001-9645-8056
Javier O CifuenteInstituto Biofi sika (UPV/EHU, CSIC), University of the Basque Country, 48940, Leioa, Spain.ORCID http://orcid.org/0000-0001-5420-121X
Weston B StruweThe Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, UK.ORCID http://orcid.org/0000-0003-0594-226X
Ricardo M BiondiInstituto de Investigación en Biomedicina de Buenos Aires (IBioBA), CONICET/Partner Institute of the Max Planck Society, Buenos Aires, Argentina.ORCID http://orcid.org/0000-0002-8873-7167
Alberto MarinaInstituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC), Valencia, Spain.ORCID http://orcid.org/0000-0002-1334-5273
Sean R ConnellStructural Biology of Cellular Machines Laboratory, Biocruces Bizkaia Health Research Institute, Cruces University Hospital, 48903, Barakaldo, Bizkaia, Spain.ORCID http://orcid.org/0000-0001-7807-7049
Justin L P BeneschThe Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, Oxford, UK.ORCID http://orcid.org/0000-0002-1507-3742
Patricia CasinoDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Spain.ORCID http://orcid.org/0000-0002-2144-188X
Christophe ColleoniUniversity of Lille, CNRS, UMR8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, Lille, France.ORCID http://orcid.org/0000-0002-6534-6120
Tom DesmetCentre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, Ghent, Belgium. tom.desmet@ugent.be.ORCID http://orcid.org/0000-0002-5788-3022
Marcelo E GuerinStructural Glycobiology Laboratory, Department of Structural and Molecular Biology, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, Barcelona, Spain. mrccri@ibmb.csic.es.ORCID http://orcid.org/0000-0001-9524-3184

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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

Indexed as

Escherichia coliEscherichia coli ProteinsGlycogen PhosphorylasePhosphoenolpyruvate Sugar Phosphotransferase SystemAllosteric RegulationBacterial ProteinsCryoelectron MicroscopyGlycogenHistidineModels, MolecularPhosphorylationBacterial ProteinsEscherichia coli ProteinsGlycogenGlycogen PhosphorylaseHistidinephosphocarrier protein HPrPhosphoenolpyruvate Sugar Phosphotransferase System

Identifiers

PMID42045210
PMCPMC13324651

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.