Evidence map›Paper›PMID 28259628›Full record

ArticleJournal of molecular biology2017

Architecture of the Flagellar Switch Complex of Escherichia coli: Conformational Plasticity of FliG and Implications for Adaptive Remodeling.

Eun A Kim, Joseph Panushka, Trevor Meyer, Ryan Carlisle, Samantha Baker, Nicholas Ide, Michael Lynch, Brian R Crane, David F Blair

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
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  13. Review
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  15. Article
  16. One Basic Blueprint, Many Different Motors.Journal of bacteriology · 2019
    Article
  17. Article
  18. Directional Switching Mechanism of the Bacterial Flagellar Motor.Computational and structural biotechnology journal · 2019
    Review
  19. Crystal structure of the FliF-FliG complex fromThe Journal of biological chemistry · 2018
    Article
  20. 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 1 country.

Eun A KimDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Joseph PanushkaDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Trevor MeyerDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Ryan CarlisleDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Samantha BakerDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Nicholas IdeDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA.
Michael LynchDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
David F BlairDepartment of Biology, University of Utah, Salt Lake City, UT 84112, USA. Electronic address: blair@bioscience.utah.edu.
University of Utah · USCornell University · US

Funding

Molecular Mechanisms of Signal Transduction Involving Light, Redox and Transmembrane ComplexesR35GM122535 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE · 2017 to 2026
$7.1M
CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
Structure and Mechanism of the Flagellar Switch ComplexR01GM064664 · NIGMS · UNIVERSITY OF UTAH · PI BLAIR, DAVID F., CRANE, BRIAN R · 2003 to 2017
$4.1M
NIGMS NIH HHS R01 GM064664NIGMS NIH HHS R35 GM122535NIGMS NIH HHS T32 GM008500
6 · The paper itself

Abstract

Structural models of the complex that regulates the direction of flagellar rotation assume either ~34 or ~25 copies of the protein FliG. Support for ~34 came from crosslinking experiments identifying an intersubunit contact most consistent with that number; support for ~25 came from the observation that flagella can assemble and rotate when FliG is genetically fused to FliF, for which the accepted number is ~25. Here, we have undertaken crosslinking and other experiments to address more fully the question of FliG number. The results indicate a copy number of ~25 for FliG. An interaction between the C-terminal and middle domains, which has been taken to support a model with ~34 copies, is also supported. To reconcile the interaction with a FliG number of ~25, we hypothesize conformational plasticity in an interdomain segment of FliG that allows some subunits to bridge gaps created by the number mismatch. This proposal is supported by mutant phenotypes and other results indicating that the normally helical segment adopts a more extended conformation in some subunits. The FliG amino-terminal domain is organized in a regular array with dimensions matching a ring in the upper part of the complex. The model predicts that FliG copy number should be tied to that of FliF, whereas FliM copy number can increase or decrease according to the number of FliG subunits that adopt the extended conformation. This has implications for the phenomenon of adaptive switch remodeling, in which the FliM copy number varies to adjust the bias of the switch.

Indexed as

Protein MultimerizationBacterial ProteinsEscherichia coli ProteinsMacromolecular SubstancesModels, BiologicalModels, MolecularProtein ConformationBacterial ProteinsEscherichia coli ProteinsFlig protein, BacteriaMacromolecular Substanceschemotaxismolecular motorsmotilityprotein structureself-assembly

Identifiers

PMID28259628
PMCPMC5494207
OpenAlexW2593220620

What OpenQuestion holds

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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.