Evidence map›Paper›PMID 28177321›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

The crystal structure of PD1, a Haemophilus surface fibril domain.

Jack Wright, Maren Thomsen, Robert Kolodziejczyk, Joshua Ridley, Jessica Sinclair, Glenn Carrington, Birendra Singh, Kristian Riesbeck, Adrian Goldman

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

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 at 2 institutions in 4 countries.

Jack WrightAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Maren ThomsenAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Robert KolodziejczykAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Joshua RidleyAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Jessica SinclairAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Glenn CarringtonAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Birendra SinghDepartment of Clinical Microbiology, Lund University, Jan Waldenströms gata 59, SE-205 02 Malmö, Sweden.
Kristian RiesbeckDepartment of Clinical Microbiology, Lund University, Jan Waldenströms gata 59, SE-205 02 Malmö, Sweden.
Adrian GoldmanAstbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
University of Leeds · GBLund University · SE

Funding

Biotechnology and Biological Sciences Research Council ALERT-13Biotechnology and Biological Sciences Research Council BB/M021610/1Wellcome TrustWellcome Trust 091322/2/10/2
6 · The paper itself

Abstract

The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel `hairpin-like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high-resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 Å resolution. The structure corrects the previous domain annotation by revealing the presence of an unexpected N-terminal TrpRing domain. PD1 represents the first Hsf domain to be solved, and thus paves the way for further research on the `hairpin-like' hypothesis.

Indexed as

Adhesins, BacterialAmino Acid SequenceBacterial AdhesionBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionHaemophilus influenzaeModels, MolecularPlasmidsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsRecombinant ProteinsAdhesins, BacterialHia adhesinHsf protein, bacteriaRecombinant Proteinsadhesincell adhesionHaemophilus influenzaeHaemophilus surface fibrilHsf putative domain 1trimeric autotransporter

Identifiers

PMID28177321
PMCPMC5297931
OpenAlexW2585920691

What OpenQuestion holds

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LicenceCC BY
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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.