Structure of photosynthetic LH1–RC supercomplex at 1.9 Å resolution

Yu, Long; Suga, Michihiro; Wang-Otomo, Zheng-Yu; Shen, Jian Ren

doi:10.1038/s41586-018-0002-9

Cited by 139 publications

(224 citation statements)

References 33 publications

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“…To cope with the various light environments where different photosynthetic organisms inhabit, different types and numbers of light‐harvesting antenna proteins are attached to the PSII core to enhance the light‐harvesting and energy‐quenching capacities . The pigments involved in energy harvesting are bacteriochlorophylls in anoxygenic photosynthetic bacteria , and mainly chlorophylls (Chl) a/b and various carotenoids in oxygenic photosynthetic organisms .…”

Section: Introductionmentioning

confidence: 99%

“…This is another important feature of FCPs, since diatoms experience a more dynamic, fluctuating light environment in water due to the continuous flow and mixing of water layers, which would require a more robust system to protect diatoms from photodamage. The outstanding ability of FCPs in absorbing blue‐green light and in dissipating excess energy may constitute one of the major reasons for diatoms to survive successfully in the aquatic environment .…”

Section: Introductionmentioning

confidence: 99%

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Structural features of the diatom photosystem II–light‐harvesting antenna complex

Wang

Zhao

et al. 2020

The FEBS Journal

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In photosynthesis, light energy is captured by pigments bound to light-harvesting antenna proteins (LHC) that then transfer the energy to the photosystem (PS) cores to initiate photochemical reactions. The LHC proteins surround the PS cores to form PS-LHC supercomplexes. In order to adapt to a wide range of light environments, photosynthetic organisms have developed a large variety of pigments and antenna proteins to utilize the light energy efficiently under different environments. Diatoms are a group of important eukaryotic algae and possess fucoxanthin (Fx) chlorophyll a/c proteins (FCP) as antenna which have exceptional capabilities of harvesting blue-green light under water and dissipate excess energy under strong light conditions. We have solved the structure of a PSII-FCPII supercomplex from a centric diatom Chaetoceros gracilis by cryo-electron microscopy, and also the structure of an isolated FCP dimer from a pennate diatom Phaeodactylum tricornutum by X-ray crystallography at a high resolution.These results revealed the oligomerization states of FCPs distinctly different from those of LHCII found in the green lineage organisms, the detailed binding patterns of Chl c and Fxs, a huge pigment network, and extensive protein-protein, pigment-protein, and pigment-pigment interactions within the PSII-FCPII supercomplex. These results therefore provide a solid structural basis for examining the detailed mechanisms of the highly efficient energy transfer and quenching processes in diatoms.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Wang

Zhao

et al. 2020

The FEBS Journal

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“…Transmembrane helix prediction on WPS-2 L and M subunits was computed using the TMHMM Server, v. 2.0 (http://www.cbs.dtu.dk/services/TMHMM/) 34 1.0 (http://dgpred.cbr.su.se/) 35 . Structural homology models were carried out with SWISS-MODEL server (https://swissmodel.expasy.org/) 36 using the 1.9 Å crystal structure of the gammaproteobacterium Thermochromatium tepidum as template 14 (PDB ID: 5y5s). The WPS-2 L and M subunits annotated as Ga0175859_11240458 and Ga0175859_11402733 respectively were used for the structural reconstruction.…”

Section: Reaction Center Evolution Analysesmentioning

confidence: 99%

“…These have traditionally been subdivided into two types, the L and M found in the reaction centers of phototrophic Proteobacteria (PbRC) and the L and M found in those of the phototrophic Chloroflexi (CfRC), with each set making separate monophyletic clades 12,13 . Therefore, substantial differences exist between the PbRC and the CfRC not only at the level of photochemistry, but also at the level of sequence identity of the core subunits, pigment and subunit composition 14,15 . Phototrophic Gemmatimonadetes, on the other hand, encode Proteobacteia-like reaction centers, as Zeng et al 10 demonstrated that this group obtained phototrophy via horizontal gene transfer of an entire photosynthesis gene cluster from a gammaproteobacterium.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary Implications of Anoxygenic Phototrophy in the Bacterial PhylumCandidatusPalusbacterota (WPS-2)

Ward

Cardona

Holland‐Moritz

2019

Preprint

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Genome-resolved environmental metagenomic sequencing has uncovered substantial previously unrecognized microbial diversity relevant for understanding the ecology and evolution of the biosphere, providing a more nuanced view of the distribution and ecological significance of traits including phototrophy across diverse niches. Recently, the capacity for bacteriochlorophyll-based anoxygenic photosynthesis has been found in the uncultured bacterial WPS-2 clade that are in close association with boreal moss. Here, we use phylogenomic analysis to investigate the diversity and evolution of phototrophic WPS-2. We demonstrate that phototrophic WPS-2 show significant genetic and metabolic divergence from other phototrophic and non-phototrophic lineages. The genomes of these organisms encode a completely new family of anoxygenic Type II photochemical reaction centers and other phototrophy-related proteins that are both phylogenetically and structurally distinct from those found in previously described phototrophs. We propose the name Candidatus Palusbacterota for the phylum-level aerobic WPS-2 clade which contains phototrophic lineages, from the Latin for "bog bacteria", distinguishing it from the anaerobic, non-phototrophic sister phylum Candidatus Eremiobacterota for "desert bacteria", typically found in dry environments.

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“…A [9], which is among the highest resolution for such a large, multi-subunit membrane-protein complex [15].…”

Section: Introductionmentioning

confidence: 99%

Novel features of LH1‐RC from Thermochromatium tepidum revealed from its atomic resolution structure

Suga

Wang-Otomo

et al. 2018

The FEBS Journal

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Light‐harvesting‐1 (LH1)‐reaction center (RC) super‐complex is a membrane protein–pigment complex existing in purple photosynthetic bacteria, where LH1 absorbs light energy and transfers them rapidly and efficiently to RC to initiate the charge separation and electron transfer reactions. The structure of LH1‐RC has been reported at relatively low resolutions from several different species of bacteria previously, but was solved at an atomic resolution recently from a thermophilic photosynthetic bacterium Thermochromatium tepidum. This high‐resolution structure revealed the detailed organization of the super‐complex including a number of unique features that are important for its functioning, such as a more intact RC structure, transporting routes for quinones to replace the bound QB as well as for the in‐and‐out of the closed LH1 ring, detailed coordinating environment of the Ca2+ ions in LH1 important for the remarkable red shift of the absorption spectrum, as well as for the enhanced thermostability. These results thus greatly advance our understanding on the mechanisms of energy transfer, quinone exchange, the red shift in the LH1‐Qy transition and the enhanced thermal stability, in this super‐complex.

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Structure of photosynthetic LH1–RC supercomplex at 1.9 Å resolution

Cited by 139 publications

References 33 publications

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Evolutionary Implications of Anoxygenic Phototrophy in the Bacterial PhylumCandidatusPalusbacterota (WPS-2)

Novel features of LH1‐RC from Thermochromatium tepidum revealed from its atomic resolution structure

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