Evidence map›Paper›PMID 37550369›Full record

ArticleNature plants2023

Cryo-EM structure of a plant photosystem II supercomplex with light-harvesting protein Lhcb8 and α-tocopherol.

Monika Opatíková, Dmitry A Semchonok, David Kopečný, Petr Ilík, Pavel Pospíšil, Iva Ilíková, Pavel Roudnický, Sanja Ćavar Zeljković, Petr Tarkowski, Fotis L Kyrilis and 3 more

Abstract read
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In one paragraph

Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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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

13 authors.

Monika Opatíková *Department of Biophysics, Faculty of Science, Palacký University, Olomouc, Czech Republic.ORCID 0000-0002-3833-6971
Dmitry A Semchonok *Interdisciplinary Research Center HALOmem, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.
David KopečnýDepartment of Experimental Biology, Faculty of Science, Palacký University, Olomouc, Czech Republic.ORCID 0000-0002-4309-4284
Petr IlíkDepartment of Biophysics, Faculty of Science, Palacký University, Olomouc, Czech Republic.ORCID 0000-0002-8929-8290
Pavel PospíšilDepartment of Biophysics, Faculty of Science, Palacký University, Olomouc, Czech Republic.ORCID 0000-0001-9126-2011
Iva IlíkováInstitute of Experimental Botany of the Czech Academy of Sciences, Centre of Plant Structural and Functional Genomics, Olomouc, Czech Republic.ORCID 0000-0002-3547-3110
Pavel RoudnickýCentral European Institute of Technology, Masaryk University, Brno, Czech Republic.ORCID 0000-0002-6904-7646
Sanja Ćavar ZeljkovićCzech Advanced Technology and Research Institute, Palacký University, Olomouc, Czech Republic.
Petr TarkowskiCzech Advanced Technology and Research Institute, Palacký University, Olomouc, Czech Republic.ORCID 0000-0002-7581-7686
Fotis L KyrilisInterdisciplinary Research Center HALOmem, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.ORCID 0000-0002-4040-6289
Farzad HamdiInterdisciplinary Research Center HALOmem, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.ORCID 0000-0002-2155-5000
Panagiotis L KastritisInterdisciplinary Research Center HALOmem, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.ORCID 0000-0002-1463-8422
Roman KouřilDepartment of Biophysics, Faculty of Science, Palacký University, Olomouc, Czech Republic. roman.kouril@upol.cz.ORCID 0000-0001-8211-3348

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 391498659Deutsche Forschungsgemeinschaft (German Research Foundation) RTG 2467EC | European Regional Development Fund (Europski Fond za Regionalni Razvoj) CZ.02.1.01/0.0/0.0/16_019/0000827EC | European Regional Development Fund (Europski Fond za Regionalni Razvoj) CZ.02.1.01/0.0/0.0/18_046/0015974Grantová Agentura České Republiky (Grant Agency of the Czech Republic) 21-05497SMinisterstvo Školství, Mládeže a Tělovýchovy (Ministry of Education, Youth and Sports) LM2023042Ministerstvo Zemědělství (Ministry of Agriculture) RO0423
6 · The paper itself

Abstract

The heart of oxygenic photosynthesis is the water-splitting photosystem II (PSII), which forms supercomplexes with a variable amount of peripheral trimeric light-harvesting complexes (LHCII). Our knowledge of the structure of green plant PSII supercomplex is based on findings obtained from several representatives of green algae and flowering plants; however, data from a non-flowering plant are currently missing. Here we report a cryo-electron microscopy structure of PSII supercomplex from spruce, a representative of non-flowering land plants, at 2.8 Å resolution. Compared with flowering plants, PSII supercomplex in spruce contains an additional Ycf12 subunit, Lhcb4 protein is replaced by Lhcb8, and trimeric LHCII is present as a homotrimer of Lhcb1. Unexpectedly, we have found α-tocopherol (α-Toc)/α-tocopherolquinone (α-TQ) at the boundary between the LHCII trimer and the inner antenna CP43. The molecule of α-Toc/α-TQ is located close to chlorophyll a614 of one of the Lhcb1 proteins and its chromanol/quinone head is exposed to the thylakoid lumen. The position of α-Toc in PSII supercomplex makes it an ideal candidate for the sensor of excessive light, as α-Toc can be oxidized to α-TQ by high-light-induced singlet oxygen at low lumenal pH. The molecule of α-TQ appears to shift slightly into the PSII supercomplex, which could trigger important structure-functional modifications in PSII supercomplex. Inspection of the previously reported cryo-electron microscopy maps of PSII supercomplexes indicates that α-Toc/α-TQ can be present at the same site also in PSII supercomplexes from flowering plants, but its identification in the previous studies has been hindered by insufficient resolution.

Indexed as

alpha-TocopherolPhotosystem II Protein ComplexCryoelectron MicroscopyPhotosynthesisPlantsThylakoidsalpha-TocopherolPhotosystem II Protein Complex

Identifiers

PMID37550369

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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.