Evidence map›Paper›PMID 27939783›Full record

ArticleStructure (London, England : 1993)2017

Structural Basis for Regulation and Specificity of Fructooligosaccharide Import in Streptococcus pneumoniae.

Simone Culurgioni, Gemma Harris, Anirudh K Singh, Samantha J King, Martin A Walsh

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Vagabond: bond-based parametrization reduces overfitting for refinement of proteins.Acta crystallographica. Section D, Structural biology · 2021
    Article
  5. Article
  6. Article
  7. Molecular analysis of an enigmaticThe Journal of biological chemistry · 2019
    Article
  8. Article
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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

5 authors at 3 institutions in 2 countries.

Simone CulurgioniDiamond House, Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK.
Gemma HarrisResearch Complex at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK.
Anirudh K SinghCenter for Microbial Pathogenesis, The Research Institute at Nationwide Children's Hospital, Columbus, OH 43205, USA.
Samantha J KingCenter for Microbial Pathogenesis, The Research Institute at Nationwide Children's Hospital, Columbus, OH 43205, USA; Department of Pediatrics, The Ohio State University College of Medicine, Columbus, OH 43210, USA.
Martin A WalshDiamond House, Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK. Electronic address: martin.walsh@diamond.ac.uk.
Nationwide Children's Hospital · USResearch Complex at Harwell · GBDiamond Light Source · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pneumoniae is dependent on carbohydrate uptake for colonization and pathogenesis, and dedicates over a third of its transport systems to their uptake. The ability of the pneumococcus to utilize fructooligosaccharides (FOSs) is attributed to the presence of one of two types of FOS ATP-binding cassette (ABC) transporters. Strains encoding SfuABC are only able to utilize short-chain FOSs, while strains encoding FusABC can utilize both short- and long-chain FOSs. The crystal structures of the substrate-binding protein FusA in its open and closed conformations bound to FOSs, and solution scattering data of SfuA, delineate the structural basis for import of short- and long-chain FOSs. The structure of FusA identifies an EF hand-like calcium-binding motif. This is shown to be essential for translocation of FOSs in FusABC and forms the basis for the definition of a new class of substrate-binding proteins that regulate substrate translocation by calcium.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsBinding SitesCalciumCrystallography, X-RayEF Hand MotifsGene Regulatory NetworksModels, MolecularOligosaccharidesProtein BindingProtein ConformationStreptococcus pneumoniaeSubstrate SpecificityATP-Binding Cassette TransportersBacterial ProteinsCalciumfructooligosaccharideOligosaccharidescalcium signalingcarbohydrate ABC transportersStreptococcus pneumoniaesubstrate-binding proteinssubstrate translocation regulation

Identifiers

PMID27939783
PMCPMC5222590
OpenAlexW2560742153

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.