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- PDB-7sa3: Structure of a monomeric photosystem II core complex from a cyano... -
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Basic information
Entry | Database: PDB / ID: 7sa3 | ||||||||||||
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Title | Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light | ||||||||||||
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Function / homology | ![]() oxygen evolving activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Gisriel, C.J. / Bryant, D.A. / Brudvig, G.W. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls d and f. Authors: Christopher J Gisriel / Gaozhong Shen / Ming-Yang Ho / Vasily Kurashov / David A Flesher / Jimin Wang / William H Armstrong / John H Golbeck / Marilyn R Gunner / David J Vinyard / Richard J ...Authors: Christopher J Gisriel / Gaozhong Shen / Ming-Yang Ho / Vasily Kurashov / David A Flesher / Jimin Wang / William H Armstrong / John H Golbeck / Marilyn R Gunner / David J Vinyard / Richard J Debus / Gary W Brudvig / Donald A Bryant / ![]() ![]() Abstract: Far-red light (FRL) photoacclimation in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include ...Far-red light (FRL) photoacclimation in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700-800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light. These new Chls effectively lower the energy canonically thought to define the "red limit" for light required to drive photochemical catalysis of water oxidation. Changes to the architecture of FRL-PSII were previously unknown, and the positions of Chl d and Chl f molecules had only been proposed from indirect evidence. Here, we describe the 2.25 Å resolution cryo-EM structure of a monomeric FRL-PSII core complex from Synechococcus sp. PCC 7335 cells that were acclimated to FRL. We identify one Chl d molecule in the Chl position of the electron transfer chain and four Chl f molecules in the core antenna. We also make observations that enhance our understanding of PSII biogenesis, especially on the acceptor side of the complex where a bicarbonate molecule is replaced by a glutamate side chain in the absence of the assembly factor Psb28. In conclusion, these results provide a structural basis for the lower energy limit required to drive water oxidation, which is the gateway for most solar energy utilization on earth. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Download
PDBx/mmCIF format | ![]() | 378.1 KB | Display | ![]() |
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PDB format | ![]() | 306.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 24943MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Photosystem II ... , 5 types, 5 molecules BCDIK
#2: Protein | ![]() Mass: 56440.980 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#3: Protein | ![]() Mass: 52375.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#4: Protein | ![]() Mass: 39596.496 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#7: Protein/peptide | ![]() Mass: 4229.917 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#8: Protein/peptide | ![]() Mass: 5069.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Cytochrome b559 subunit ... , 2 types, 2 molecules EF
#5: Protein | ![]() Mass: 9136.276 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#6: Protein/peptide | ![]() Mass: 5023.960 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein / Protein/peptide , 2 types, 2 molecules AN
#1: Protein | Mass: 40111.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#9: Protein/peptide | Mass: 1975.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Sugars , 2 types, 8 molecules ![](data/chem/img/LMT.gif)
![](data/chem/img/DGD.gif)
![](data/chem/img/DGD.gif)
#16: Sugar | ChemComp-LMT / #18: Sugar | |
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-Non-polymers , 13 types, 278 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/CLA.gif)
![](data/chem/img/CL7.gif)
![](data/chem/img/PHO.gif)
![](data/chem/img/BCR.gif)
![](data/chem/img/LMG.gif)
![](data/chem/img/FE2.gif)
![](data/chem/img/PL9.gif)
![](data/chem/img/LHG.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/CLA.gif)
![](data/chem/img/CL7.gif)
![](data/chem/img/PHO.gif)
![](data/chem/img/BCR.gif)
![](data/chem/img/LMG.gif)
![](data/chem/img/FE2.gif)
![](data/chem/img/PL9.gif)
![](data/chem/img/LHG.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/HOH.gif)
#10: Chemical | ChemComp-CA / | ||||||||||||||||||||
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#11: Chemical | ChemComp-CL / ![]() | ||||||||||||||||||||
#12: Chemical | ChemComp-CLA / ![]() #13: Chemical | ChemComp-CL7 / | ![]() #14: Chemical | ![]() #15: Chemical | ChemComp-BCR / ![]() #17: Chemical | ChemComp-F6C / ![]() #19: Chemical | #20: Chemical | ChemComp-FE2 / | #21: Chemical | ChemComp-PL9 / | ![]() #22: Chemical | ChemComp-LHG / | ![]() #23: Chemical | ChemComp-HEM / | ![]() #24: Water | ChemComp-HOH / | ![]() |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: ![]() |
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Sample preparation
Component | Name: Monomeric photosystem II from cyanobacteria acclimated to far-red light![]() Type: COMPLEX / Entity ID: #1-#9 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 6.5 |
Specimen | Conc.: 3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Specimen support | Details: 25 mA / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: C-flat-2/1 |
Vitrification![]() | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Image recording | Electron dose: 40.8 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction![]() | Resolution: 2.25 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 315307 / Symmetry type: POINT |