Evidence map›Paper›PMID 34272394›Full record

ArticleNature communications2021

The molecular basis of regulation of bacterial capsule assembly by Wzc.

Yun Yang, Jiwei Liu, Bradley R Clarke, Laura Seidel, Jani R Bolla, Philip N Ward, Peijun Zhang, Carol V Robinson, Chris Whitfield, James H Naismith

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

47 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  3. Hypermucoviscosity inJournal of bacteriology · 2026
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  5. Genomic Analysis of HypervirulentIranian journal of biotechnology · 2026
    Article
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  18. 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

10 authors at 3 institutions in 2 countries.

Yun Yang *Rosalind Franklin Institute, Harwell Campus, Harwell, UK.
Jiwei Liu *Rosalind Franklin Institute, Harwell Campus, Harwell, UK.
Bradley R ClarkeDepartment of Molecular and Cellular Biology, The University of Guelph, Guelph, ON, Canada.ORCID 0000-0003-2233-1268
Laura SeidelDepartment of Molecular and Cellular Biology, The University of Guelph, Guelph, ON, Canada.
Jani R BollaPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, South Parks Road, The University of Oxford, Oxford, UK.ORCID 0000-0003-4346-182X
Philip N WardRosalind Franklin Institute, Harwell Campus, Harwell, UK.ORCID 0000-0003-2546-3426
Peijun ZhangDivision of Structural Biology, The University of Oxford, Oxford, UK.ORCID 0000-0003-1803-691X
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, South Parks Road, The University of Oxford, Oxford, UK.ORCID 0000-0001-7829-5505
Chris WhitfieldDepartment of Molecular and Cellular Biology, The University of Guelph, Guelph, ON, Canada. cwhitfie@uoguelph.ca.ORCID 0000-0002-5267-7027
James H NaismithRosalind Franklin Institute, Harwell Campus, Harwell, UK. naismith@strubi.ox.ac.uk.ORCID 0000-0001-6744-5061
University of Oxford · GBUniversity of Guelph · CADiamond Light Source · GB

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
Biotechnology and Biological Sciences Research CouncilCIHR FDN-2016-148364Medical Research Council MR/N020413/1Medical Research Council MR/V028839/1NIGMS NIH HHS P50 GM082251Wellcome TrustWellcome Trust 100209/Z/12/ZWellcome Trust 20289/Z16/ZWellcome Trust 206422/Z/17/Z
6 · The paper itself

Abstract

Bacterial extracellular polysaccharides (EPSs) play critical roles in virulence. Many bacteria assemble EPSs via a multi-protein "Wzx-Wzy" system, involving glycan polymerization at the outer face of the cytoplasmic/inner membrane. Gram-negative species couple polymerization with translocation across the periplasm and outer membrane and the master regulator of the system is the tyrosine autokinase, Wzc. This near atomic cryo-EM structure of dephosphorylated Wzc from E. coli shows an octameric assembly with a large central cavity formed by transmembrane helices. The tyrosine autokinase domain forms the cytoplasm region, while the periplasmic region contains small folded motifs and helical bundles. The helical bundles are essential for function, most likely through interaction with the outer membrane translocon, Wza. Autophosphorylation of the tyrosine-rich C-terminus of Wzc results in disassembly of the octamer into multiply phosphorylated monomers. We propose that the cycling between phosphorylated monomer and dephosphorylated octamer regulates glycan polymerization and translocation.

Indexed as

Amino Acid MotifsBacterial CapsulesCatalytic DomainCryoelectron MicroscopyCytoplasmEscherichia coliEscherichia coli ProteinsMass SpectrometryMembrane ProteinsModels, MolecularPeriplasmPhosphorylationPolysaccharides, BacterialProtein Conformation, alpha-HelicalProtein-Tyrosine KinasesTyrosineEscherichia coli ProteinsMembrane ProteinsPolysaccharides, BacterialProtein-Tyrosine KinasesTyrosinewzc protein, E coli

Identifiers

PMID34272394
PMCPMC8285477
OpenAlexW3178310686

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.