Evidence map›Paper›PMID 26095026›Full record

ArticleStructure (London, England : 1993)2015

Light Signaling Mechanism of Two Tandem Bacteriophytochromes.

Xiaojing Yang, Emina A Stojković, Wesley B Ozarowski, Jane Kuk, Erna Davydova, Keith Moffat

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
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  7. Article
  8. Deconvolution of dynamic heterogeneity in protein structure.Structural dynamics (Melville, N.Y.) · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
  19. 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

6 authors.

Xiaojing YangDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA; Department of Ophthalmology and Vision Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA. Electronic address: xiaojing@uic.edu.
Emina A StojkovićDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; Department of Biology, Northeastern Illinois University, Chicago, IL 60625, USA.
Wesley B OzarowskiDepartment of Biology, Northeastern Illinois University, Chicago, IL 60625, USA.
Jane KukDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Erna DavydovaDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Keith MoffatDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA; Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA. Electronic address: moffat@cars.uchicago.edu.

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR01GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1986 to 2012
$4.7M
Structures, Dynamics and Signaling Mechanisms of Modular PhotoreceptorsR01EY024363 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YANG, XIAOJING · 2014 to 2021
$2.9M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR37GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1995 to 2004
$1.9M
BioCARS: A Synchroton Structural Biology ResourceP41GM103543 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2012 to 2012
$1.1M
NCRR NIH HHS P41 RR007707NEI NIH HHS R01 EY024363NEI NIH HHS R01EY024363NIGMS NIH HHS GM036452NIGMS NIH HHS GM103543NIGMS NIH HHS R01 GM036452NIGMS NIH HHS R37 GM036452
6 · The paper itself

Abstract

RpBphP2 and RpBphP3, two tandem bacteriophytochromes from the photosynthetic bacterium Rhodopseudomonas palustris, share high sequence identity but exhibit distinct photoconversion behavior. Unlike the canonical RpBphP2, RpBphP3 photoconverts to an unusual near-red-absorbing (Pnr) state; both are required for synthesis of light-harvesting complexes under low-light conditions. Here we report the crystal structures of the photosensory core modules of RpBphP2 and RpBphP3. Despite different quaternary structures, RpBphP2 and RpBphP3 adopt nearly identical tertiary structures. The RpBphP3 structure reveals tongue-and-groove interactions at the interface between the GAF and PHY domains. A single mutation in the PRxSF motif at the GAF-PHY interface abolishes light-induced formation of the Pnr state in RpBphP3, possibly due to altered structural rigidity of the chromophore-binding pocket. Structural comparisons suggest that long-range signaling involves structural rearrangement of the helical spine at the dimer interface. These structures, together with mutational studies, provide insights into photoconversion and the long-range signaling mechanism in phytochromes.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayHydrogen BondingLight Signal TransductionModels, MolecularMolecular Sequence DataPhytochromeProtein Structure, SecondaryProtein Structure, TertiaryRhodopseudomonasBacterial ProteinsPhytochrome

Identifiers

PMID26095026
PMCPMC4497868

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.