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Yorodumi- EMDB-51788: Cryo EM structure of RC-dLH complex model II from Gemmatimonas gr... -
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Open data
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Basic information
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| Title | Cryo EM structure of RC-dLH complex model II from Gemmatimonas groenlandica | |||||||||
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Keywords | photosynthetic bacteria / photosynthesis / reaction cennter light harvesting complex / RC-LH1 / RC-dLH / cryo-EM / Gemmatimonas groenlandica | |||||||||
| Function / homology | Function and homology informationorganelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / endomembrane system / electron transfer activity / iron ion binding / heme binding / metal ion binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | Gemmatimonas groenlandica (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||
Authors | Gardiner AT / Jing Y / Bina D / Mujakic I / Gardian Z / Kaftan D / Joosten M / Jakobi A / Castro-Hartmann P / Qian P / Koblizek M | |||||||||
| Funding support | Czech Republic, 1 items
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Citation | Journal: mSystems / Year: 2026Title: Two solutions for efficient light-harvesting in phototrophic . Authors: Alastair T Gardiner / Yibo Jin / David Bína / Maarten Joosten / David Kaftan / Izabela Mujakić / Zdenko Gardian / Pablo Castro-Hartmann / Pu Qian / Michal Koblížek / ![]() Abstract: Phototrophic Gemmatimonadota represent a unique group of phototrophic bacteria that acquired a complete set of photosynthetic genes via horizontal gene transfer and later evolved independently. () ...Phototrophic Gemmatimonadota represent a unique group of phototrophic bacteria that acquired a complete set of photosynthetic genes via horizontal gene transfer and later evolved independently. () contains photosynthetic complexes with two concentric light-harvesting antenna rings that absorb at 816 and 868 nm, allowing it to better exploit the light conditions found deeper in the water column. The closely related species , with highly similar photosynthetic genes, harvests infrared light using a single 860 nm absorption band. The cryo-electron microscopy structure of the photosynthetic complex reveals that the outer antenna lacks monomeric bacteriochlorophylls, resulting in a smaller optical antenna cross-section. The spectrum is red-shifted relative to due to the formation of a H-bond enabled by a different rotamer conformation of αTrp in the outer ring. This H-bond forms with a neighboring bacteriochlorophyll and increases the intra-dimer exciton coupling, affecting the exciton localization probability within the rings and increasing exciton cooperativity between the complexes. The functional consequences of the spectral shift, caused solely by a subtle conformational change of a single residue, represent a novel mechanism in which phototrophic organisms adjust their antennae for particular light conditions and enable to grow higher in the water column where more photons are available.IMPORTANCEThe photoheterotrophic species of the phylum Gemmatimonadota employ unique photosynthetic complexes with two concentric antenna rings around a central reaction center. In contrast to other phototrophic species, these organisms have not evolved any regulatory systems to control the expression of their photosynthetic apparatus under different light conditions. Despite the overall similarity, the complexes present in and have different absorption properties in the near-infrared region of the spectrum that make them more suitable for low or medium light, respectively. The main difference in absorption depends on the conformation of a single tryptophan residue that can form an H-bond with a neighboring bacteriochlorophyll. The presence or absence of this H-bond affects how the protein scaffold interacts with the bacteriochlorophylls, which in turn determines how light energy is transferred within and between the photosynthetic complexes. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51788.map.gz | 777.7 MB | EMDB map data format | |
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| Header (meta data) | emd-51788-v30.xml emd-51788.xml | 37.6 KB 37.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51788_fsc.xml | 19.8 KB | Display | FSC data file |
| Images | emd_51788.png | 49.7 KB | ||
| Filedesc metadata | emd-51788.cif.gz | 9.2 KB | ||
| Others | emd_51788_half_map_1.map.gz emd_51788_half_map_2.map.gz | 764.3 MB 764.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51788 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51788 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9h22MC ![]() 9h19C 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_51788.map.gz / Format: CCP4 / Size: 824 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: 0.732 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_51788_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_51788_half_map_2.map | ||||||||||||
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Sample components
+Entire : RC-dLH complex model II from Gemmatimonas groenlandica
+Supramolecule #1: RC-dLH complex model II from Gemmatimonas groenlandica
+Macromolecule #1: reaction centre S sub unit
+Macromolecule #2: Reaction center protein L chain
+Macromolecule #3: Reaction center protein M chain
+Macromolecule #4: reaction centre Ht su unit
+Macromolecule #5: reaction centre Hc sub unit
+Macromolecule #6: Photosynthetic reaction center cytochrome c subunit
+Macromolecule #7: Light-harvesting protein
+Macromolecule #8: Light-harvesting protein
+Macromolecule #9: Light-harvesting protein
+Macromolecule #10: BACTERIOCHLOROPHYLL A
+Macromolecule #11: BACTERIOPHEOPHYTIN A
+Macromolecule #12: DODECYL-BETA-D-MALTOSIDE
+Macromolecule #13: MENAQUINONE 8
+Macromolecule #14: FE (III) ION
+Macromolecule #15: (2R,5R,11R,14R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-2,14-bis(te...
+Macromolecule #16: SPIRILLOXANTHIN
+Macromolecule #17: 1,2-DIDECANOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
+Macromolecule #18: HEME C
+Macromolecule #19: (2~{E},4~{E},6~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{...
+Macromolecule #20: water
-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 / Details: 10mM Tris-HCl buffer, 20 mM NaCl, pH 8.0 |
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III / Details: blot time, 3 sec blot force, 3. |
| Details | in buffer solution with detergent beta-DDM. ~4 mg/ml |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Temperature | Min: 88.0 K / Max: 92.0 K |
| Specialist optics | Energy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV |
| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 23012 / Average exposure time: 5.13 sec. / Average electron dose: 60.0 e/Å2 / Details: images were collected in AFIS model |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 165000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Details | Initial model was established with coot. The model was fitted into map using chimera. The refinement was performed y the use of Phenix. |
| Refinement | Space: REAL / Protocol: RIGID BODY FIT / Overall B value: 60 / Target criteria: map to model |
| Output model | ![]() PDB-9h22: |
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About Yorodumi



Keywords
Gemmatimonas groenlandica (bacteria)
Authors
Czech Republic, 1 items
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FIELD EMISSION GUN

