Evidence map›Paper›PMID 26163297›Full record

ArticleBMC structural biology2015

Structure of the stationary phase survival protein YuiC from B.subtilis.

Doris H X Quay, Ambrose R Cole, Adam Cryar, Konstantinos Thalassinos, Mark A Williams, Sanjib Bhakta, Nicholas H Keep

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Frontiers in microbiology · 2018
    Article
  4. Expression ofBiotechnology for biofuels · 2017
    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

7 authors at 3 institutions in 1 country.

Doris H X QuayInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. d.quay@mail.cryst.bbk.ac.uk.
Ambrose R ColeInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. a.cole@mail.cryst.bbk.ac.uk.
Adam CryarInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London, WC1E 6BT, UK. a.cryar@ucl.ac.uk.
Konstantinos ThalassinosInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. k.thalassinos@ucl.ac.uk.
Mark A WilliamsInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. m.williams@mail.cryst.bbk.ac.uk.
Sanjib BhaktaInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. s.bhakta@bbk.ac.uk.
Nicholas H KeepInstitute for Structural and Molecular Biology, Crystallography, Department of Biological Sciences, Birkbeck University of London, Malet Street, London, WC1E 7HX, UK. n.keep@mail.cryst.bbk.ac.uk.
Birkbeck, University of London · GBInstitute of Structural and Molecular Biology · GBUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F011148/1Biotechnology and Biological Sciences Research Council BB/F016948/1Medical Research Council G0401038
6 · The paper itself

Abstract

backgroundStationary phase survival proteins (Sps) were found in Firmicutes as having analogous domain compositions, and in some cases genome context, as the resuscitation promoting factors of Actinobacteria, but with a different putative peptidoglycan cleaving domain.

resultsThe first structure of a Firmicute Sps protein YuiC from B. subtilis, is found to be a stripped down version of the cell-wall peptidoglycan hydrolase MltA. The YuiC structures are of a domain swapped dimer, although some monomer is also found in solution. The protein crystallised in the presence of pentasaccharide shows a 1,6-anhydrodisaccharide sugar product, indicating that YuiC cleaves the sugar backbone to form an anhydro product at least on lengthy incubation during crystallisation.

conclusionsThe structural simplification of MltA in Sps proteins is analogous to that of the resuscitation promoting factor domains of Actinobacteria, which are stripped down versions of lysozyme and soluble lytic transglycosylase proteins.

Indexed as

Acid PhosphataseBacillus subtilisBacterial ProteinsCatalytic DomainCrystallography, X-RayGlycosyltransferasesModels, MolecularOligosaccharidesProtein Structure, SecondaryAcid PhosphataseBacterial ProteinsGlycosyltransferasesMltA protein, bacteriaOligosaccharides

Identifiers

PMID26163297
PMCPMC4499186
OpenAlexW1842908127

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.