Evidence map›Paper›PMID 39915441›Full record

ArticleNature communications2025

A distinct double-ring LH1-LH2 photocomplex from an extremophilic phototroph.

Kazutoshi Tani, Kenji V P Nagashima, Risa Kojima, Masaharu Kondo, Ryo Kanno, Issei Satoh, Mai Kawakami, Naho Hiwatashi, Kazuna Nakata, Sakiko Nagashima and 14 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

24 authors.

Kazutoshi Tani *Center for Computational Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan. ktani@ccs.tsukuba.ac.jp.ORCID http://orcid.org/0000-0003-4835-154X
Kenji V P Nagashima *Research Institute for Integrated Science, Kanagawa University, Yokohama, Kanagawa, Japan.
Risa Kojima *College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.ORCID http://orcid.org/0009-0008-7325-0170
Masaharu Kondo *Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya, Aichi, Japan.ORCID http://orcid.org/0000-0003-2914-2662
Ryo KannoQuantum Wave Microscopy Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Kunigami-gun, Okinawa, Japan.
Issei SatohFaculty of Science, Ibaraki University, Mito, Japan.
Mai KawakamiFaculty of Science, Ibaraki University, Mito, Japan.
Naho HiwatashiFaculty of Science, Ibaraki University, Mito, Japan.
Kazuna NakataDepartment of Agrobioscience, Graduate School of Agriculture, Kobe University, Kobe, Japan.
Sakiko NagashimaResearch Institute for Integrated Science, Kanagawa University, Yokohama, Kanagawa, Japan.ORCID http://orcid.org/0009-0000-4720-6346
Kazuhito InoueResearch Institute for Integrated Science, Kanagawa University, Yokohama, Kanagawa, Japan.
Yugo IsawaCollege of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan.
Ryoga MorishitaDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya, Aichi, Japan.
Shinichi TakaichiDepartment of Molecular Microbiology, Faculty of Life Science, Tokyo University of Agriculture, Setagaya, Tokyo, Japan.ORCID http://orcid.org/0000-0002-1621-9141
Endang R PurbaScientific Imaging Section, Okinawa Institute of Science and Technology Graduate University (OIST), Kunigami-gun, Okinawa, Japan.
Malgorzata HallScientific Imaging Section, Okinawa Institute of Science and Technology Graduate University (OIST), Kunigami-gun, Okinawa, Japan.
Long-Jiang YuKey Laboratory of Photobiology, Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-4962-1049
Michael T MadiganSchool of Biological Sciences, Department of Microbiology, Southern Illinois University, Carbondale, IL, USA.
Akira MizoguchiGraduate School of Medicine, Mie University, Tsu, Japan.
Bruno M HumbelProvost Office, Okinawa Institute of Science and Technology Graduate University (OIST), Kunigami-gun, Okinawa, Japan.ORCID http://orcid.org/0000-0002-7095-1368
Yukihiro KimuraDepartment of Agrobioscience, Graduate School of Agriculture, Kobe University, Kobe, Japan. ykimura@people.kobe-u.ac.jp.ORCID http://orcid.org/0000-0003-3747-0367
Yutaka NagasawaCollege of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan. ynagasa@fc.ritsumei.ac.jp.ORCID http://orcid.org/0000-0002-9154-4585
Takehisa DewaDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya, Aichi, Japan. takedewa@nitech.ac.jp.ORCID http://orcid.org/0000-0002-9786-3114
Zheng-Yu Wang-OtomoFaculty of Science, Ibaraki University, Mito, Japan. wang@ml.ibaraki.ac.jp.ORCID http://orcid.org/0000-0003-1676-2002

Funding

Japan Society for the Promotion of Science London (JSPS London) 20H02856Japan Society for the Promotion of Science London (JSPS London) 24K01620
6 · The paper itself

Abstract

Halorhodospira (Hlr.) halophila strain BN9622 is an extremely halophilic and alkaliphilic phototrophic purple sulfur bacterium isolated from a hypersaline lake in the Libyan Desert whose total salinity exceeded 35% at pH 10.7. Here we present a cryo-EM structure of the native LH1-LH2 co-complex from strain BN9622 at 2.22 Å resolution. Surprisingly, the LH1-LH2 co-complex consists of a double-ring cylindrical structure with the larger LH1 ring encircling a smaller LH2 ring. The Hlr. halophila LH1 contains 18 αβ-subunits and additional bacteriochlorophyll a (BChl a) molecules that absorb maximally at 797 nm. The LH2 ring is composed of 9 αβ-subunits, and the BChl a molecules in the co-complex form extensive intra- and inter-complex networks to allow near 100% efficiency of energy transfer to its surrounding LH1. The additional LH1-B797 BChls a are located in such a manner that they facilitate exciton transfer from monomeric BChls in LH2 to the dimeric BChls in LH1. The structural features of the strain BN9622 LH1-LH2 co-complex may have evolved to allow a minimal LH2 complex to maximize excitation transfer to the core complex and effectively harvest light in the physiologically demanding ecological niche of this purple bacterium.

Indexed as

Bacterial ProteinsExtremophilesLight-Harvesting Protein ComplexesBacteriochlorophyll ACryoelectron MicroscopyModels, MolecularBacterial ProteinsBacteriochlorophyll ALight-Harvesting Protein Complexes

Identifiers

PMID39915441
PMCPMC11802735

What OpenQuestion holds

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Registered trials

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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.