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Yorodumi- EMDB-14528: Cryo-EM structure of the whole photosynthetic complex from the gr... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-14528 | |||||||||
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Title | Cryo-EM structure of the whole photosynthetic complex from the green sulfur bacteria | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information thylakoid / bacteriochlorophyll binding / iron-sulfur cluster binding / photosynthesis / electron transfer activity / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Chlorobaculum tepidum TLS (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.5 Å | |||||||||
Authors | Xie H / Tsiotis G | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2023 Title: Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium . Authors: Hao Xie / Alexandros Lyratzakis / Radhika Khera / Myrto Koutantou / Sonja Welsch / Hartmut Michel / Georgios Tsiotis / Abstract: Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the ...Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna-Matthews-Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from at 2.5 Å resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of energy from antenna to the electron transport chain of this RC and the transfer of electrons from reduced sulfur compounds to the special pair. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_14528.map.gz | 168.1 MB | EMDB map data format | |
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Header (meta data) | emd-14528-v30.xml emd-14528.xml | 23.8 KB 23.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_14528_fsc.xml | 12.4 KB | Display | FSC data file |
Images | emd_14528.png | 143.3 KB | ||
Others | emd_14528_half_map_1.map.gz emd_14528_half_map_2.map.gz | 165 MB 165 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-14528 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14528 | HTTPS FTP |
-Validation report
Summary document | emd_14528_validation.pdf.gz | 849.5 KB | Display | EMDB validaton report |
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Full document | emd_14528_full_validation.pdf.gz | 849.1 KB | Display | |
Data in XML | emd_14528_validation.xml.gz | 20.3 KB | Display | |
Data in CIF | emd_14528_validation.cif.gz | 26.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14528 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14528 | HTTPS FTP |
-Related structure data
Related structure data | 7z6qMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_14528.map.gz / Format: CCP4 / Size: 178 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: 0.837 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_14528_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_14528_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Photosystem P840 reaction center
+Supramolecule #1: Photosystem P840 reaction center
+Macromolecule #1: Photosystem P840 reaction center, large subunit
+Macromolecule #2: Photosystem P840 reaction center iron-sulfur protein
+Macromolecule #3: Cytochrome c
+Macromolecule #4: P840 reaction center 17 kDa protein
+Macromolecule #5: Bacteriochlorophyll a protein
+Macromolecule #6: Bacteriochlorophyll A isomer
+Macromolecule #7: CHLOROPHYLL A
+Macromolecule #8: BACTERIOCHLOROPHYLL A
+Macromolecule #9: [(2R,3S,4S,5R,6R)-6-[(10E,12E,14E)-2,6,10,14,19,23-hexamethyl-25-...
+Macromolecule #10: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
+Macromolecule #11: [(2~{R})-2-hexadecanoyloxy-3-[(2~{S},3~{S},4~{R},5~{R},6~{S})-6-(...
+Macromolecule #12: CALCIUM ION
+Macromolecule #13: IRON/SULFUR CLUSTER
+Macromolecule #14: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 0.2 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 4 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 4092 pixel / Digitization - Dimensions - Height: 5769 pixel / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated defocus max: 2.5 µm / Calibrated defocus min: 1.2 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |