Evidence map›Paper›PMID 31501441›Full record

ArticleNature communications2019

Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio.

Richard W Meek, Ian T Cadby, Patrick J Moynihan, Andrew L Lovering

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Ocular Delivery of Predatory Bacteria with Cryomicroneedles Against Eye Infection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
    Article
  10. Article
  11. Open biology · 2021
    Article
  12. Article
  13. The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020
    Review
  14. Article
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

4 authors at 1 institution in 1 country.

Richard W MeekInstitute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Ian T CadbyInstitute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0002-3135-6769
Patrick J MoynihanInstitute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0003-4182-6223
Andrew L LoveringInstitute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK. a.lovering@bham.ac.uk.ORCID http://orcid.org/0000-0002-1856-7975
University of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N011945/1Biotechnology and Biological Sciences Research Council BB/S010122/1
6 · The paper itself

Abstract

The bacterial second messenger cyclic-di-GMP is a widespread, prominent effector of lifestyle change. An example of this occurs in the predatory bacterium Bdellovibrio bacteriovorus, which cycles between free-living and intraperiplasmic phases after entering (and killing) another bacterium. The initiation of prey invasion is governed by DgcB (GGDEF enzyme) that produces cyclic-di-GMP in response to an unknown stimulus. Here, we report the structure of DgcB, and demonstrate that the GGDEF and sensory forkhead-associated (FHA) domains form an asymmetric dimer. Our structures indicate that the FHA domain is a consensus phosphopeptide sensor, and that the ligand for activation is surprisingly derived from the N-terminal region of DgcB itself. We confirm this hypothesis by determining the structure of a FHA:phosphopeptide complex, from which we design a constitutively-active mutant (confirmed via enzyme assays). Our results provide an understanding of the stimulus driving DgcB-mediated prey invasion and detail a unique mechanism of GGDEF enzyme regulation.

Indexed as

Amino Acid SequenceBacterial ProteinsBdellovibrioEnzyme ActivationEscherichia coli ProteinsLigandsModels, MolecularMutant ProteinsPhosphopeptidesPhosphorus-Oxygen LyasesProtein DomainsProtein MultimerizationStructure-Activity RelationshipBacterial Proteinsdiguanylate cyclaseEscherichia coli ProteinsLigandsMutant ProteinsPhosphopeptidesPhosphorus-Oxygen Lyases

Identifiers

PMID31501441
PMCPMC6733907
OpenAlexW2973204810

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.