- EMDB-55593: Chlorophyll f-containing dimeric far-red Photosystem II from Chro... -
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Basic information
Entry
Database: EMDB / ID: EMD-55593
Title
Chlorophyll f-containing dimeric far-red Photosystem II from Chroococcidiopsis thermalis PCC 7203
Map data
Sample
Complex: Dimeric far-red Photosystem II
Protein or peptide: x 21 types
Ligand: x 18 types
Keywords
Chlorophyll f / photosystem II / ELECTRON TRANSPORT / FaRLiP
Function / homology
Function and homology information
photosystem II oxygen evolving complex / photosystem II assembly / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / photosynthetic electron transport chain / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosystem II / response to herbicide ...photosystem II oxygen evolving complex / photosystem II assembly / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / photosynthetic electron transport chain / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosystem II / response to herbicide / extrinsic component of membrane / plasma membrane-derived thylakoid membrane / photosynthetic electron transport in photosystem II / chlorophyll binding / photosynthesis, light reaction / phosphate ion binding / photosynthesis / respiratory electron transport chain / manganese ion binding / electron transfer activity / protein stabilization / iron ion binding / heme binding / metal ion binding Similarity search - Function
Photosystem II protein Y (PsbY) / Photosystem II PsbY / Photosystem II PsbU, oxygen evolving complex / Photosystem II 12 kDa extrinsic protein (PsbU) / Photosystem II PsbV, cytochrome c-550 precursor / Photosystem II cytochrome c-550 precursor / Cytochrome c-550 domain / Cytochrome c-550 domain / Photosystem II PsbX, type 1 subfamily / Photosystem II PsbJ ...Photosystem II protein Y (PsbY) / Photosystem II PsbY / Photosystem II PsbU, oxygen evolving complex / Photosystem II 12 kDa extrinsic protein (PsbU) / Photosystem II PsbV, cytochrome c-550 precursor / Photosystem II cytochrome c-550 precursor / Cytochrome c-550 domain / Cytochrome c-550 domain / Photosystem II PsbX, type 1 subfamily / Photosystem II PsbJ / Photosystem II PsbJ superfamily / PsbJ / Photosystem II PsbO, manganese-stabilising / Manganese-stabilising protein / photosystem II polypeptide / Photosystem II reaction centre protein Ycf12 / Photosystem II complex subunit Ycf12 / Photosystem II reaction centre M protein (PsbM) / Photosystem II PsbM superfamily / Photosystem II PsbM / Photosystem II PsbZ, reaction centre / Photosystem II PsbZ superfamily / YCF9 / Photosystem II PsbX / Photosystem II reaction centre X protein (PsbX) / Photosystem II PsbT / Photosystem II PsbL / Photosystem II CP43 reaction centre protein / Photosystem II PsbL superfamily / Photosystem II PsbT superfamily / Photosystem II CP43 reaction centre protein superfamily / Photosystem II reaction centre T protein / PsbL protein / Photosystem II PsbK / Photosystem II PsbK superfamily / Photosystem II 4 kDa reaction centre component / Photosystem II PsbI / Photosystem II CP47 reaction centre protein / Photosystem II PsbI superfamily / Photosystem II reaction centre I protein (PSII 4.8 kDa protein) / Photosystem II protein D1 / Photosystem II reaction centre protein H / Photosystem II D2 protein / Photosystem II cytochrome b559, conserved site / Photosystem II cytochrome b559, alpha subunit / Photosystem II cytochrome b559, beta subunit / Photosystem II cytochrome b559, N-terminal / Photosystem II cytochrome b559, alpha subunit, lumenal region / Photosystem II reaction centre protein H superfamily / Photosystem II cytochrome b559, alpha subunit superfamily / Cytochrome b559, alpha (gene psbE) and beta (gene psbF)subunits / Lumenal portion of Cytochrome b559, alpha (gene psbE) subunit / Photosystem II 10 kDa phosphoprotein / Cytochrome b559 subunits heme-binding site signature. / : / Photosystem antenna protein-like / Photosystem antenna protein-like superfamily / Photosystem II protein / Outer membrane protein/outer membrane enzyme PagP, beta-barrel / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Prokaryotic membrane lipoprotein lipid attachment site profile. Similarity search - Domain/homology
Photosystem II reaction center protein I / Photosystem II reaction center protein K / Photosystem II extrinsic protein V / Photosystem II CP43 reaction center protein / Photosystem II reaction center protein Psb30 / Photosystem II protein D1 / Photosystem II phosphoprotein PsbH / Photosystem II CP47 reaction center protein / Photosystem II extrinsic protein O / Photosystem II D2 protein ...Photosystem II reaction center protein I / Photosystem II reaction center protein K / Photosystem II extrinsic protein V / Photosystem II CP43 reaction center protein / Photosystem II reaction center protein Psb30 / Photosystem II protein D1 / Photosystem II phosphoprotein PsbH / Photosystem II CP47 reaction center protein / Photosystem II extrinsic protein O / Photosystem II D2 protein / Uncharacterized protein / Photosystem II reaction center protein L / Cytochrome b559 subunit beta / Photosystem II reaction center protein J / Cytochrome b559 subunit alpha / Photosystem II extrinsic protein U / Photosystem II reaction center protein Y / Photosystem II reaction center protein Z / Photosystem II reaction center protein X / Photosystem II reaction center protein M / Photosystem II reaction center protein T Similarity search - Component
Biological species
Chroococcidiopsis thermalis PCC 7203 (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 2.17 Å
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/M011178/1
United Kingdom
Royal Society
RSRP/S2/242010
United Kingdom
H2020 Marie Curie Actions of the European Commission
955520
European Union
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/R001383/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/V002015/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/R00921X
United Kingdom
Leverhulme Trust
RPG-2022-203
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/Z516740/1
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
UKRI2820
United Kingdom
Imperial College London
Presidents PhD Scholarship
United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/X019284/1
United Kingdom
Citation
Journal: Nat Commun / Year: 2026 Title: Mapping the absorption landscape of far-red Photosystem II. Authors: Ho Fong Leong / Giovanni Consoli / Geoffry A Davis / Ben Hancox-Lachman / Kenta Renard / Fiazall Tufail / Lauren E Lee / Lucas Gautier / James W Murray / Andrea Fantuzzi / A William Rutherford / Abstract: Far-red light photoacclimation enables some cyanobacteria to survive in white-light-depleted environments by extending the red limit of photosynthesis. In far-red Photosystem II, paralogous subunits ...Far-red light photoacclimation enables some cyanobacteria to survive in white-light-depleted environments by extending the red limit of photosynthesis. In far-red Photosystem II, paralogous subunits replace their canonical counterparts, allowing the incorporation of some chlorophyll f molecules and one chlorophyll d that are red-shifted and spectrally distinct from the chlorophyll a manifold, and from each other. Here, we present a comparative study of far-red Photosystem II from Chroococcidiopsis thermalis PCC 7203 and Calothrix sp. NIES-3974. In C. thermalis, the cryo-electron microscopy structure reveals the far-red-exclusive subunit, PsbH2', which forms part of a chlorophyll f binding site. We also assign four chlorophyll f sites using sequence comparisons and electrostatic potential analyses. In Calothrix, psbH2' is absent, and the same analyses show that only two of these chlorophyll f sites are present. Comparative phylogenetic, structural, and spectroscopic analyses allow the assignment of specific wavelengths to all the red-shifted chlorophylls. This provides the framework needed to model excitation energy transfer in far-red Photosystem II, and to understand the conserved features that allow survival under far-red light.
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