Evidence map›Paper›PMID 18468622›Full record

ArticleJournal of molecular biology2008

Determination of the physiological dimer interface of the PhoQ sensor domain.

Shalom D Goldberg, Cinque S Soto, Carey D Waldburger, William F Degrado

Abstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  13. Article
  14. 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

4 authors.

Shalom D GoldbergDepartment of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Cinque S Soto
Carey D Waldburger
William F Degrado

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
Design and mechanistic studies of mimics of antimicrobial peptidesR01AI074866 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2008 to 2012
$3.0M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
Design and mechanistic studies of mimics of antimicrobial peptidesR56AI074866 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DEGRADO, WILLIAM · 2013 to 2013
$573k
Computational Design of Proteins with Enzymatic ActivityF32GM073499 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GOLDBERG, SHALOM D · 2005 to 2007
$118k
NIAID NIH HHS AI74866NIAID NIH HHS R01 AI074866NIAID NIH HHS R56 AI074866NIGMS NIH HHS F32 GM073499NIGMS NIH HHS GM073499NIGMS NIH HHS GM54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

PhoQ is the transmembrane sensor kinase of the phoPQ two-component system, which detects and responds to divalent cations and antimicrobial peptides and can trigger bacterial virulence. Despite their ubiquity and importance in bacterial signaling, the structure and molecular mechanism of the sensor kinases is not fully understood. Frequently, signals are transmitted from a periplasmic domain in these proteins to the cytoplasmic kinase domains via an extended dimeric interface, and the PhoQ protein would appear to follow this paradigm. However, the isolated truncated periplasmic domain of PhoQ dimerizes poorly, so it has been difficult to distinguish the relevant interface in crystal structures of the PhoQ periplasmic domain. Thus, to determine the arrangement of the periplasmic domains of Escherichia coli PhoQ in the physiological homodimer, disulfide-scanning mutagenesis was used. Single cysteine substitutions were introduced along the N-terminal helix of the periplasmic region, and the degree of cross-linking in each protein variant was determined by Western blotting and immunodetection. The results were subjected to periodicity analysis to generate a profile that provides information concerning the C(beta) distances between corresponding residues at the interface. This profile, together with a rigid-body search procedure, side-chain placement, and energy minimization, was used to build a model of the dimer arrangement. The final model proved to be highly compatible with one of the PhoQ crystal structures, 3BQ8, indicating that 3BQ8 is representative of the physiological arrangement. The model of the periplasmic region is also compatible with a full-length PhoQ protein in which a four-helix bundle forms in the membrane. The membrane four-helix bundle has been proposed for other sensor kinases and is thought to have a role in the mechanism of signal transduction; our model supports the idea that signaling through a membrane four-helix bundle is a widespread mechanism in the transmembrane sensor kinases.

Indexed as

Bacterial ProteinsCysteineDimerizationEscherichia coliEscherichia coli ProteinsModels, MolecularMutagenesis, Site-DirectedProtein Structure, TertiaryRecombinant ProteinsBacterial ProteinsCysteineEscherichia coli ProteinsPhoQ protein, BacteriaRecombinant Proteins

Identifiers

PMID18468622
PMCPMC2542651

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.