Evidence map›Paper›PMID 28977623›Full record

ArticleNucleic acids research2017

Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.

Grecia M Gonzalez, Svetlana Durica-Mitic, Steven W Hardwick, Martin C Moncrieffe, Marcus Resch, Piotr Neumann, Ralf Ficner, Boris Görke, Ben F Luisi

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  11. Article
  12. The Natural AntimicrobialFoods (Basel, Switzerland) · 2021
    Article
  13. A SpontaneousmSphere · 2021
    Article
  14. Spontaneous Phage Resistance in Avian PathogenicFrontiers in microbiology · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

9 authors.

Grecia M GonzalezDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Svetlana Durica-MiticDepartment of Microbiology, Immunology and Genetics, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter, 1030 Vienna, Austria.
Steven W HardwickDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Martin C MoncrieffeDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Marcus ReschGeorg-August University Göttingen, Department of Molecular Structural Biology Justus von Liebig Weg 11, D-37077 Göttingen, Germany.
Piotr NeumannGeorg-August University Göttingen, Department of Molecular Structural Biology Justus von Liebig Weg 11, D-37077 Göttingen, Germany.
Ralf FicnerGeorg-August University Göttingen, Department of Molecular Structural Biology Justus von Liebig Weg 11, D-37077 Göttingen, Germany.
Boris GörkeDepartment of Microbiology, Immunology and Genetics, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter, 1030 Vienna, Austria.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.

Funding

Austrian Science Fund FWF P 26681Wellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

In phylogenetically diverse bacteria, the conserved protein RapZ plays a central role in RNA-mediated regulation of amino-sugar metabolism. RapZ contributes to the control of glucosamine phosphate biogenesis by selectively presenting the regulatory small RNA GlmZ to the essential ribonuclease RNase E for inactivation. Here, we report the crystal structures of full length Escherichia coli RapZ at 3.40 Å and 3.25 Å, and its isolated C-terminal domain at 1.17 Å resolution. The structural data confirm that the N-terminal domain of RapZ possesses a kinase fold, whereas the C-terminal domain bears closest homology to a subdomain of 6-phosphofructokinase, an important enzyme in the glycolytic pathway. RapZ self-associates into a domain swapped dimer of dimers, and in vivo data support the importance of quaternary structure in RNA-mediated regulation of target gene expression. Based on biochemical, structural and genetic data, we suggest a mechanism for binding and presentation by RapZ of GlmZ and the closely related decoy sRNA, GlmY. We discuss a scenario for the molecular evolution of RapZ through re-purpose of enzyme components from central metabolism.

Indexed as

Amino SugarsEndoribonucleasesEscherichia coliEscherichia coli ProteinsModels, MolecularMutationProtein BindingProtein DomainsProtein MultimerizationRNARNA-Binding ProteinsRNA, Small UntranslatedAmino SugarsEndoribonucleasesEscherichia coli Proteinsribonuclease ERNARNA-Binding ProteinsRNA, Small UntranslatedYhbJ protein, E coli

Identifiers

PMID28977623
PMCPMC5737377

What OpenQuestion holds

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LicenceCC BY
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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.