Evidence map›Paper›PMID 40168055›Full record

ArticleeLife2025

Structure of the Calvin-Benson-Bassham sedoheptulose-1,7-bisphosphatase from the model microalga

Théo Le Moigne, Martina Santoni, Lucile Jomat, Stéphane D Lemaire, Mirko Zaffagnini, Nicolas Chéron, Julien Henri

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2025. 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

7 authors.

Théo Le MoigneSorbonne Université, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, Institut de Biologie Paris-Seine, Paris, France.
Martina SantoniSorbonne Université, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, Institut de Biologie Paris-Seine, Paris, France.
Lucile JomatSorbonne Université, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, Institut de Biologie Paris-Seine, Paris, France.
Stéphane D LemaireSorbonne Université, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, Institut de Biologie Paris-Seine, Paris, France.
Mirko ZaffagniniDepartment of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy.
Nicolas ChéronPASTEUR, Département de chimie, École Normale Supérieure (ENS), PSL University, Sorbonne Université, CNRS UMR8640, Paris, France.
Julien HenriSorbonne Université, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, Institut de Biologie Paris-Seine, Paris, France.ORCID https://orcid.org/0000-0003-0772-8881

Funding

Agence Nationale de la Recherche ANR-19-CE11-0009Centre National de la Recherche Scientifique INSB-D-2022-135GENCI-IDRIS 2021-077156Sorbonne University ERASMUS+University of Bologna ERASMUS+
6 · The paper itself

Abstract

The Calvin-Benson-Bassham cycle (CBBC) performs carbon fixation in photosynthetic organisms. Among the eleven enzymes that participate in the pathway, sedoheptulose-1,7-bisphosphatase (SBPase) is expressed in photo-autotrophs and catalyzes the hydrolysis of sedoheptulose-1,7-bisphosphate (SBP) to sedoheptulose-7-phosphate (S7P). SBPase, along with nine other enzymes in the CBBC, contributes to the regeneration of ribulose-1,5-bisphosphate, the carbon-fixing co-substrate used by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The metabolic role of SBPase is restricted to the CBBC, and a recent study revealed that the three-dimensional structure of SBPase from the moss

Indexed as

Chlamydomonas reinhardtiiPhosphoric Monoester HydrolasesCrystallography, X-RayModels, MolecularPhotosynthesisProtein ConformationPhosphoric Monoester Hydrolasessedoheptulose-bisphosphatasechlamydomonas reinhardtiicrystallographyintegrative structural biologymolecular biophysicsmolecular dynamicsphotosynthesisplant biologyprotein-protein interactionredox post-translational modificationstructural biology

Identifiers

PMID40168055
PMCPMC11961124

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.