Evidence map›Paper›PMID 31570616›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.

Ciaran R McFarlane, Nita R Shah, Burak V Kabasakal, Blanca Echeverria, Charles A R Cotton, Doryen Bubeck, James W Murray

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.9field-weighted citation impact, top 5% of its field
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

49 citing papers in PubMed, 98 citations in OpenAlex.

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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 at 1 institution in 1 country.

Ciaran R McFarlaneDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom.
Nita R ShahDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom.
Burak V KabasakalDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom.
Blanca EcheverriaDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom.
Charles A R CottonDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom.
Doryen BubeckDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom d.bubeck@imperial.ac.uk j.w.murray@imperial.ac.uk.ORCID 0000-0001-8241-9697
James W MurrayDepartment of Life Sciences, Imperial College London, SW7 2AZ, United Kingdom d.bubeck@imperial.ac.uk j.w.murray@imperial.ac.uk.ORCID 0000-0002-8897-0161
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014575/1Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Plants, algae, and cyanobacteria fix carbon dioxide to organic carbon with the Calvin-Benson (CB) cycle. Phosphoribulokinase (PRK) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) are essential CB-cycle enzymes that control substrate availability for the carboxylation enzyme Rubisco. PRK consumes ATP to produce the Rubisco substrate ribulose bisphosphate (RuBP). GAPDH catalyzes the reduction step of the CB cycle with NADPH to produce the sugar glyceraldehyde 3-phosphate (GAP), which is used for regeneration of RuBP and is the main exit point of the cycle. GAPDH and PRK are coregulated by the redox state of a conditionally disordered protein CP12, which forms a ternary complex with both enzymes. However, the structural basis of CB-cycle regulation by CP12 is unknown. Here, we show how CP12 modulates the activity of both GAPDH and PRK. Using thermophilic cyanobacterial homologs, we solve crystal structures of GAPDH with different cofactors and CP12 bound, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide preorders CP12 prior to binding the PRK active site, which is resolved in complex with CP12. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our structural and biochemical data explain how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation.

Indexed as

Bacterial ProteinsCyanobacteriaGlyceraldehyde 3-PhosphateGlyceraldehyde-3-Phosphate DehydrogenasesLightNADPOxidation-ReductionPhosphotransferases (Alcohol Group Acceptor)PhotosynthesisProtein BindingRibulose-Bisphosphate CarboxylaseThermosynechococcusBacterial ProteinsGlyceraldehyde 3-PhosphateGlyceraldehyde-3-Phosphate DehydrogenasesNADPphosphoribulokinasePhosphotransferases (Alcohol Group Acceptor)Ribulose-Bisphosphate CarboxylaseCalvin–Benson cyclecarbon fixationphotosynthesisredox regulation

Identifiers

PMID31570616
PMCPMC6800369
OpenAlexW2977304844

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.