+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0834 | |||||||||
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Title | Structure of the peripheral FCPI from diatom | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Chaetoceros gracilis (Diatom) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
Authors | Nagao R / Kato K / Miyazaki N / Akita F / Shen JR | |||||||||
Citation | Journal: Nat Commun / Year: 2020 Title: Structural basis for assembly and function of a diatom photosystem I-light-harvesting supercomplex. Authors: Ryo Nagao / Koji Kato / Kentaro Ifuku / Takehiro Suzuki / Minoru Kumazawa / Ikuo Uchiyama / Yasuhiro Kashino / Naoshi Dohmae / Seiji Akimoto / Jian-Ren Shen / Naoyuki Miyazaki / Fusamichi Akita / Abstract: Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c- ...Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c-binding proteins (FCPs) present in diatoms, a group of organisms having important contribution to the global carbon cycle. Here, we report a 2.40-Å resolution structure of the diatom photosystem I (PSI)-FCPI supercomplex by cryo-electron microscopy. The supercomplex is composed of 16 different FCPI subunits surrounding a monomeric PSI core. Each FCPI subunit showed different protein structures with different pigment contents and binding sites, and they form a complicated pigment-protein network together with the PSI core to harvest and transfer the light energy efficiently. In addition, two unique, previously unidentified subunits were found in the PSI core. The structure provides numerous insights into not only the light-harvesting strategy in diatom PSI-FCPI but also evolutionary dynamics of light harvesters among oxyphototrophs. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_0834.map.gz | 28.8 MB | EMDB map data format | |
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Header (meta data) | emd-0834-v30.xml emd-0834.xml | 23.8 KB 23.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_0834_fsc.xml | 17.7 KB | Display | FSC data file |
Images | emd_0834.png | 77.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0834 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0834 | HTTPS FTP |
-Validation report
Summary document | emd_0834_validation.pdf.gz | 344.3 KB | Display | EMDB validaton report |
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Full document | emd_0834_full_validation.pdf.gz | 343.9 KB | Display | |
Data in XML | emd_0834_validation.xml.gz | 15.9 KB | Display | |
Data in CIF | emd_0834_validation.cif.gz | 22.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0834 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0834 | HTTPS FTP |
-Related structure data
Related structure data | 6l4tMC 0835C 6l4uC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_0834.map.gz / Format: CCP4 / Size: 488.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.113 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : peripheral FCPI
+Supramolecule #1: peripheral FCPI
+Macromolecule #1: Fucoxanthin chlorophyll a/c-binding protein Lhcr12
+Macromolecule #2: Fucoxanthin chlorophyll a/c-binding protein Lhcr10
+Macromolecule #3: Fucoxanthin chlorophyll a/c-binding protein Lhcr4
+Macromolecule #4: Fucoxanthin chlorophyll a/c-binding protein Lhcr3
+Macromolecule #5: Fucoxanthin chlorophyll a/c-binding protein Lhcq13
+Macromolecule #6: Fucoxanthin chlorophyll a/c-binding protein Lhcq3
+Macromolecule #7: Fucoxanthin chlorophyll a/c-binding protein Lhcq11
+Macromolecule #8: Fucoxanthin chlorophyll a/c-binding protein Lhcq10
+Macromolecule #9: Fucoxanthin chlorophyll a/c-binding protein Lhcq8
+Macromolecule #10: Fucoxanthin chlorophyll a/c-binding protein Lhcq5
+Macromolecule #11: CHLOROPHYLL A
+Macromolecule #12: Chlorophyll c1
+Macromolecule #13: (3S,3'R,5R,6S,7cis)-7',8'-didehydro-5,6-dihydro-5,6-epoxy-beta,be...
+Macromolecule #14: (3S,3'S,5R,5'R,6S,6'R,8'R)-3,5'-dihydroxy-8-oxo-6',7'-didehydro-5...
+Macromolecule #15: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
+Macromolecule #16: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
+Macromolecule #17: DODECYL-BETA-D-MALTOSIDE
+Macromolecule #18: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 2 mg/mL | |||||||||
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Buffer | pH: 6.5 Component:
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Grid | Model: C-flat-1.2/1.3 / Material: MOLYBDENUM / Mesh: 300 / Support film - Material: CARBON / Pretreatment - Type: PLASMA CLEANING | |||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-6l4t: |