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Yorodumi- EMDB-62419: Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 comp... -
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Basic information
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| Title | Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na-containing solutions | |||||||||
Map data | Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na solutions | |||||||||
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Keywords | Photosynthesis / Reaction center / energy transfer | |||||||||
| Function / homology | Function and homology informationorganelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / electron transfer activity / iron ion binding / heme binding ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / electron transfer activity / iron ion binding / heme binding / metal ion binding / membrane / plasma membrane Similarity search - Function | |||||||||
| Biological species | Dinoroseobacter shibae DFL 12 = DSM 16493 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.78 Å | |||||||||
Authors | Chen JH | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Adv Sci (Weinh) / Year: 2025Title: Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae. Authors: Weiwei Wang / Yanting Liu / Jiayi Gu / Shaoya An / Cheng Ma / Haichun Gao / Nianzhi Jiao / Jian-Ren Shen / John Thomas Beatty / Michal Koblížek / Xing Zhang / Qiang Zheng / Jing-Hua Chen / ![]() Abstract: The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy ...The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg or Ca. The periplasmic Cyt c is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_62419.map.gz | 32.5 MB | EMDB map data format | |
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| Header (meta data) | emd-62419-v30.xml emd-62419.xml | 28 KB 28 KB | Display Display | EMDB header |
| Images | emd_62419.png | 31.2 KB | ||
| Filedesc metadata | emd-62419.cif.gz | 7.6 KB | ||
| Others | emd_62419_half_map_1.map.gz emd_62419_half_map_2.map.gz | 59.3 MB 59.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62419 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62419 | HTTPS FTP |
-Validation report
| Summary document | emd_62419_validation.pdf.gz | 961.6 KB | Display | EMDB validaton report |
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| Full document | emd_62419_full_validation.pdf.gz | 961.3 KB | Display | |
| Data in XML | emd_62419_validation.xml.gz | 12.5 KB | Display | |
| Data in CIF | emd_62419_validation.cif.gz | 14.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62419 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62419 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9km0MC ![]() 8yy9C ![]() 8yz2C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_62419.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na solutions | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.2 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex...
| File | emd_62419_half_map_1.map | ||||||||||||
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| Annotation | Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na solutions-halfmap-A | ||||||||||||
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| Density Histograms |
-Half map: Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex...
| File | emd_62419_half_map_2.map | ||||||||||||
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| Annotation | Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na solutions-halfmap-B | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : tri-heme cytochrome-associated RC-LH1 complex
+Supramolecule #1: tri-heme cytochrome-associated RC-LH1 complex
+Macromolecule #1: Antenna pigment protein alpha chain
+Macromolecule #2: Reaction center protein O chain
+Macromolecule #3: Antenna pigment protein beta chain
+Macromolecule #4: Reaction center protein M chain
+Macromolecule #5: Reaction center protein L chain
+Macromolecule #6: Reaction center protein H chain
+Macromolecule #7: Photosynthetic reaction center cytochrome c subunit
+Macromolecule #8: BACTERIOCHLOROPHYLL A
+Macromolecule #9: (4~{E},16~{E},26~{E})-2-methoxy-2,6,10,14,19,23,27,31-octamethyl-...
+Macromolecule #10: (21R,24R,27S)-24,27,28-trihydroxy-18,24-dioxo-19,23,25-trioxa-24l...
+Macromolecule #11: DODECYL-BETA-D-MALTOSIDE
+Macromolecule #12: FE (III) ION
+Macromolecule #13: UBIQUINONE-10
+Macromolecule #14: BACTERIOPHEOPHYTIN A
+Macromolecule #15: CARDIOLIPIN
+Macromolecule #16: HEME C
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / 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 / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Dinoroseobacter shibae DFL 12 = DSM 16493 (bacteria)
Authors
China, 1 items
Citation









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Processing
FIELD EMISSION GUN
