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Yorodumi- PDB-9hd7: Cryo-EM structure of photosystem II C2S2M2L2 supercomplex from th... -
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Basic information
| Entry | Database: PDB / ID: 9hd7 | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of photosystem II C2S2M2L2 supercomplex from the green alga Chlorella ohadii | ||||||||||||||||||||||||
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Keywords | MEMBRANE PROTEIN / supercomplex / photosynthesis / chlorophyll / algae | ||||||||||||||||||||||||
| Function / homology | Function and homology informationchloroplast thylakoid / eukaryotic translation initiation factor 2 complex / photosynthesis, light harvesting / photosystem II oxygen evolving complex / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / eukaryotic 48S preinitiation complex / transcription factor TFIIA complex ...chloroplast thylakoid / eukaryotic translation initiation factor 2 complex / photosynthesis, light harvesting / photosystem II oxygen evolving complex / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / eukaryotic 48S preinitiation complex / transcription factor TFIIA complex / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosynthetic electron transport chain / photosystem I / photosystem II / response to herbicide / extrinsic component of membrane / photosynthetic electron transport in photosystem II / chlorophyll binding / phosphate ion binding / photosynthesis, light reaction / chloroplast thylakoid membrane / photosynthesis / translation initiation factor activity / cell redox homeostasis / transcription initiation at RNA polymerase II promoter / ribosome binding / electron transfer activity / protein stabilization / iron ion binding / heme binding / calcium ion binding / RNA binding / metal ion binding Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Chlorella ohadii (plant) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.95 Å | ||||||||||||||||||||||||
Authors | Kopecny, D. / Kouril, R. / Ardhad, R. / Skalidis, I. / Kastritis, P. | ||||||||||||||||||||||||
| Funding support | Czech Republic, Germany, European Union, 6items
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Citation | Journal: Nat Commun / Year: 2026Title: Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance. Authors: Rameez Arshad / Ioannis Skalidis / David Kopečný / Sylva Brabencová / Monika Opatíková / Petr Ilík / Pavel Pospíšil / Farzad Hamdi / Sanja Ćavar Zeljković / Martina Kopečná / ...Authors: Rameez Arshad / Ioannis Skalidis / David Kopečný / Sylva Brabencová / Monika Opatíková / Petr Ilík / Pavel Pospíšil / Farzad Hamdi / Sanja Ćavar Zeljković / Martina Kopečná / Pavel Roudnický / Dušan Lazár / Eduard Elias / Roberta Croce / Panagiotis L Kastritis / Roman Kouřil / ![]() Abstract: Photosystem II (PSII) is essential for energy conversion during oxygenic photosynthesis in plants and algae. Chlorella ohadii, one of the fastest multiplying green algae, thrives under the harsh ...Photosystem II (PSII) is essential for energy conversion during oxygenic photosynthesis in plants and algae. Chlorella ohadii, one of the fastest multiplying green algae, thrives under the harsh desert sun but lacks the standard PSII photoprotective mechanisms involving LhcSR/PsbS proteins or protein phosphorylation. Here, we present the cryo-EM structure of the PSII supercomplex from C. ohadii at 2.9 Å resolution, which is used to determine whether the exceptional resistance to desert conditions has a structural basis in PSII. The structure reveals a distinct PsbO isoform and additional subunits, PsbR and PsbY, which enhance core complex stability through extensive interactions. Furthermore, the trimeric light-harvesting complexes (LHCII) are bound to the PSII core by specific light-harvesting proteins whose down-regulation in response to high-light conditions implies a reduction in the number of bound LHCII trimers. These structural modifications, together with the high accumulation of specific polyamines in the thylakoid membrane, play a key role in maintaining PSII stability and photoprotection, allowing C. ohadii to survive in extreme conditions. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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| PDBx/mmCIF format | 9hd7.cif.gz | 2.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9hd7.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9hd7.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hd/9hd7 ftp://data.pdbj.org/pub/pdb/validation_reports/hd/9hd7 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52056MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Assembly
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Components
-Protein , 5 types, 14 molecules 141114Gg78PpUuWw
| #1: Protein | Mass: 26744.256 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Details: GenBank accession XHY80384 / Source: (natural) Chlorella ohadii (plant)#4: Protein | Mass: 14953.089 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A5P4NAS4#19: Protein | Mass: 94779.070 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0AAD5H4X0 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5H4X0#24: Protein | Mass: 36784.391 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot accession A0A5P4NEE0 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A5P4NEE0#26: Protein | Mass: 49141.957 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0AAD5DZE4 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5DZE4 |
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-Chlorophyll a-b binding protein, ... , 6 types, 16 molecules 251215Nn361316RrSsYy
| #2: Protein | Mass: 26604.174 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5DLH1#3: Protein | Mass: 27506.311 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt accession A0AAD5DXI2 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5DXI2#5: Protein | Mass: 26169.717 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5H446#21: Protein | Mass: 31706.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0AAD5E2W2 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5E2W2#22: Protein | Mass: 30853.070 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: GenBank accession XJP35395 / Source: (natural) Chlorella ohadii (plant)#28: Protein | Mass: 27530.293 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt accession A0AAD5DNU0 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5DNU0 |
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-Photosystem II ... , 14 types, 28 molecules AaBbCcDdHhIiJjKkLlMmTtVvXxZz
| #6: Protein | Mass: 39040.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SIR2, photosystem II#7: Protein | Mass: 56199.801 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8TIK4#8: Protein | Mass: 52106.496 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: GenBank accession AII02053 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A076EAP1#9: Protein | Mass: 39534.211 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SYD4, photosystem II#12: Protein | Mass: 8575.999 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SIT0#13: Protein/peptide | Mass: 4386.098 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt acession A0A5P4ND48 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A5P4ND48#14: Protein/peptide | Mass: 4246.948 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt accession W8TIH6 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8TIH6#15: Protein/peptide | Mass: 4681.705 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0A076EAP2 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: P56348#16: Protein/peptide | Mass: 4391.162 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot W8SKK5 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: P56339#17: Protein/peptide | Mass: 3751.495 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0A5P4NAV9 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A5P4NAV9#23: Protein/peptide | Mass: 3605.399 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt W8SY98 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: P56327#25: Protein/peptide | Mass: 3450.207 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0A076EAR3 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A076EAR3#27: Protein | Mass: 9831.387 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0AAD5H2N2 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0AAD5H2N2#29: Protein | Mass: 6727.147 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt accession W8SKL0 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SKL0 |
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-Cytochrome b559 subunit ... , 2 types, 4 molecules EeFf
| #10: Protein | Mass: 9449.626 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SU91#11: Protein/peptide | Mass: 4722.640 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlorella ohadii (plant) / References: UniProt: W8SIQ3 |
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-Chloroplast oxygen-evolving enhancer protein ... , 2 types, 4 molecules OoQq
| #18: Protein | Mass: 31559.590 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: GenBank accession XHY80383 / Source: (natural) Chlorella ohadii (plant)#20: Protein | Mass: 21618.646 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: UniProt A0A5P4NB29 / Source: (natural) Chlorella ohadii (plant) / References: UniProt: A0A5P4NB29 |
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-Sugars , 1 types, 8 molecules 
| #46: Sugar | ChemComp-DGD / |
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-Non-polymers , 20 types, 604 molecules 






































| #30: Chemical | ChemComp-CHL / #31: Chemical | ChemComp-CLA / #32: Chemical | ChemComp-LHG / #33: Chemical | ChemComp-LUT / ( #34: Chemical | ChemComp-NEX / ( #35: Chemical | ChemComp-XAT / ( #36: Chemical | ChemComp-3PH / #37: Chemical | #38: Chemical | ChemComp-PHO / #39: Chemical | ChemComp-BCR / #40: Chemical | ChemComp-SQD / #41: Chemical | ChemComp-LMG / #42: Chemical | ChemComp-PL9 / |
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Chlorella ohadii (plant)
Czech Republic,
Germany, European Union, 6items
Citation


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