Evidence map›Paper›PMID 17693513›Full record

ArticleJournal of bacteriology2007

Organization of the aerotaxis receptor aer in the membrane of Escherichia coli.

Divya N Amin, Barry L Taylor, Mark S Johnson

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

3 authors.

Divya N AminDivision of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350, USA.
Barry L Taylor
Mark S Johnson

Funding

SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS GM29481NIGMS NIH HHS R01 GM029481
6 · The paper itself

Abstract

The Aer receptor guides Escherichia coli to specific oxygen and energy-generating niches. The input sensor in Aer is a flavin adenine dinucleotide-binding PAS domain, which is separated from a HAMP/signaling output domain by two membrane-spanning segments that flank a short (four-amino-acid) periplasmic loop. In this study, we determined the overall membrane organization of Aer by introducing combinations of residues that allowed us to differentiate intradimeric collisions from interdimeric collisions. Collisions between proximal residues in the membrane anchor were exclusively intra- or interdimeric but, with one exception, not both. Cross-linking profiles were consistent, with a rigid rather than flexible periplasmic loop and a tilted TM2 helix that crossed TM2' at residue V197C, near the center of the lipid bilayer. The periplasmic loop formed a stable neighborhood that (i) included a maximum of three Aer dimers, (ii) did not swap neighbors over time, and (iii) appeared to be constrained by interactions in the cytosolic signaling domain.

Indexed as

Protein Structure, QuaternaryCarrier ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsIntercellular Signaling Peptides and ProteinsMembrane ProteinsMultiprotein ComplexesMutagenesis, Site-DirectedProtein BindingProtein Interaction MappingProtein Structure, SecondaryAer protein, E coliCarrier ProteinsEscherichia coli ProteinsIntercellular Signaling Peptides and ProteinsMembrane ProteinsMultiprotein Complexes

Identifiers

PMID17693513
PMCPMC2168431

What OpenQuestion holds

Textmetadata
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.