Evidence map›Paper›PMID 42260277›Full record

ArticleCommunications chemistry2026

A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy.

Prabin Karki, William C Budell, Rohit Kannachel, David Menendez, Carolina Hernandez, Joshua H Mendez, Shemiran Kanou, Manjeet Singh, Chavdar Slavov, Peter Schwander and 3 more

Abstract read
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In one paragraph

Article in Communications chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Prabin KarkiDepartment of Physics and Astronomy, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.ORCID http://orcid.org/0009-0001-6011-7548
William C BudellNew York Structural Biology Center, New York, NY, USA.ORCID http://orcid.org/0000-0002-5538-668X
Rohit KannachelNew York Structural Biology Center, New York, NY, USA.ORCID http://orcid.org/0009-0007-0502-2769
David MenendezDepartment of Biology, Northeastern Illinois University, Chicago, IL, USA.ORCID http://orcid.org/0009-0006-9680-029X
Carolina HernandezNew York Structural Biology Center, New York, NY, USA.
Joshua H MendezNew York Structural Biology Center, New York, NY, USA.ORCID http://orcid.org/0000-0002-3317-5654
Shemiran KanouDepartment of Biology, Northeastern Illinois University, Chicago, IL, USA.
Manjeet SinghDepartment of Chemistry, University of South Florida, Tampa, FL, USA.ORCID http://orcid.org/0000-0003-0564-1686
Chavdar SlavovDepartment of Chemistry, University of South Florida, Tampa, FL, USA.ORCID http://orcid.org/0000-0001-9441-0243
Peter SchwanderDepartment of Physics and Astronomy, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.ORCID http://orcid.org/0000-0003-2350-8838
Tek Narsingh MallaVaccine Research Center Electron Microscopy Unit, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.ORCID http://orcid.org/0000-0002-1387-0801
Emina A StojkovićDepartment of Biology, Northeastern Illinois University, Chicago, IL, USA. e-stojkovic@neiu.edu.ORCID http://orcid.org/0000-0002-4971-5213
Marius SchmidtDepartment of Physics and Astronomy, University of Wisconsin-Milwaukee, Milwaukee, WI, USA. smarius@uwm.edu.ORCID http://orcid.org/0000-0002-0962-9468

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
NIGMS NIH HHS P41 GM103310
6 · The paper itself

Abstract

Phytochromes are dimeric photoreceptors found in bacteria, fungi, and plants that reversibly interconvert between a red-absorbing Pr state and a far-red-absorbing Pfr state. In bacteria, phytochromes (BphPs) regulate diverse responses through a two-component signaling pathway comprising a C-terminal histidine kinase (HK) and a response regulator. A previous cryo-EM study of the wild-type BphP from Stigmatella aurantiaca (SaBphP2) revealed a stable Pr/Pfr heterodimer in which the two protomers adopt distinct Pr and Pfr conformations. Here, using the Spotiton technique, we captured the same heterodimer by illuminating SaBphP2 particles on the cryo-EM grid and vitrifying them 10 ms later. Comparison with the Pr/Pr homodimer reveals a 180° rotation of the HK domain, driven by an unwinding of the coiled-coil helices that connect the photosensory core to the enzymatic domain. The large-scale reorientations provide mechanistic insight into light-triggered signal transduction mediated by bacterial phytochromes.

Identifiers

PMID42260277
PMCPMC13578443

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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.