Mutant structure of metabolic switch protein in complex with monomeric c-di-GMP reveals a potential mechanism of protein-mediated ligand dimerization.

Badri Nath Dubey, Viktoriya Shyp, Geoffrey Fucile, Holger Sondermann, Urs Jenal, Tilman Schirmer

Open access · goldAbstract read

In one paragraph

Article in Scientific reports, 2023. 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

0.6field-weighted citation impact, top 25% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

6 authors at 2 institutions in 2 countries.

Badri Nath DubeyBiozentrum, University of Basel, CH-4056, Basel, Switzerland. badri.nath.dubey@desy.de.

Viktoriya ShypBiozentrum, University of Basel, CH-4056, Basel, Switzerland.

Geoffrey FucilesciCORE Center for Scientific Computing, University of Basel, CH-4056, Basel, Switzerland.

Holger SondermannCSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607, Hamburg, Germany.

Urs JenalBiozentrum, University of Basel, CH-4056, Basel, Switzerland.

Tilman SchirmerBiozentrum, University of Basel, CH-4056, Basel, Switzerland.

University of Basel · CHDeutsches Elektronen-Synchrotron DESY · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial second messengers c-di-GMP and (p)ppGpp have broad functional repertoires ranging from growth and cell cycle control to the regulation of biofilm formation and virulence. The recent identification of SmbA, an effector protein from Caulobacter crescentus that is jointly targeted by both signaling molecules, has opened up studies on how these global bacterial networks interact. C-di-GMP and (p)ppGpp compete for the same SmbA binding site, with a dimer of c-di-GMP inducing a conformational change that involves loop 7 of the protein that leads to downstream signaling. Here, we report a crystal structure of a partial loop 7 deletion mutant, SmbA

Indexed as

Cyclic GMPGuanosine PentaphosphateBacterial ProteinsDimerizationLigandsBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPGuanosine PentaphosphateLigands

Identifiers

PMID36810577

DOI10.1038/s41598-023-29110-0

PMCPMC9944927

OpenAlexW4321455353

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.