Evidence map›Paper›PMID 21733840›Full record

ArticleThe Journal of biological chemistry2011

Structural and functional studies on the N-terminal domain of the Shigella type III secretion protein MxiG.

Melanie A McDowell, Steven Johnson, Janet E Deane, Martin Cheung, A Dorothea Roehrich, Ariel J Blocker, James M McDonnell, Susan M Lea

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  17. The blueprint of the type-3 injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
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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

8 authors at 2 institutions in 1 country.

Melanie A McDowellSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Steven JohnsonSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Janet E DeaneSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Martin CheungSchools of Cellular and Molecular Medicine and Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
A Dorothea RoehrichSchools of Cellular and Molecular Medicine and Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
Ariel J BlockerSchools of Cellular and Molecular Medicine and Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
James M McDonnellDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom. Electronic address: susan.lea@path.ox.ac.uk.
University of Oxford · GBUniversity of Bristol · GB

Funding

Medical Research Council G0401595Medical Research Council G1000758Wellcome Trust 059011Wellcome Trust 086833
6 · The paper itself

Abstract

MxiG is a single-pass membrane protein that oligomerizes within the inner membrane ring of the Shigella flexneri type III secretion system (T3SS). The MxiG N-terminal domain (MxiG-N) is the predominant cytoplasmic structure; however, its role in T3SS assembly and secretion is largely uncharacterized. We have determined the solution structure of MxiG-N residues 6-112 (MxiG-N(6-112)), representing the first published structure of this T3SS domain. The structure shows strong structural homology to forkhead-associated (FHA) domains. Canonically, these cell-signaling modules bind phosphothreonine (Thr(P)) via highly conserved residues. However, the putative phosphate-binding pocket of MxiG-N(6-112) does not align with other FHA domain structures or interact with Thr(P). Furthermore, mutagenesis of potential phosphate-binding residues has no effect on S. flexneri T3SS assembly and function. Therefore, MxiG-N has a novel function for an FHA domain. Positioning of MxiG-N(6-112) within the EM density of the S. flexneri needle complex gives insight into the ambiguous stoichiometry of the T3SS, supporting models with 24 MxiG subunits in the inner membrane ring.

Indexed as

Bacterial ProteinsBinding SitesCloning, MolecularCongo RedConserved SequenceFluorescent DyesMagnetic Resonance SpectroscopyMembrane ProteinsModels, BiologicalModels, MolecularMolecular ConformationMutagenesis, Site-DirectedMutationPhosphatesPhosphothreonineProtein Structure, SecondaryBacterial ProteinsCongo RedFluorescent DyesMembrane ProteinsPhosphatesPhosphothreonine

Identifiers

PMID21733840
PMCPMC3162421
OpenAlexW1997959554

What OpenQuestion holds

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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.