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Yorodumi- EMDB-65526: LH2 complex from Ectothiorhodospira haloalkaliphila with inhibite... -
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Open data
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Basic information
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| Title | LH2 complex from Ectothiorhodospira haloalkaliphila with inhibited carotenoid biosynthesis | |||||||||
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Keywords | PHOTOSYNTHESIS / Light-harvesing / purple sulfur bacteria / cryo-EM | |||||||||
| Function / homology | Function and homology informationplasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / metal ion binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 1.92 Å | |||||||||
Authors | Burtseva AD / Baymukhametov TN / Popov VO / Ashikhmin AA / Boyko KM | |||||||||
| Funding support | Russian Federation, 1 items
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Citation | Journal: FEBS Lett / Year: 2025Title: Structural insights into LH2 complexes formed by a purple sulfur bacterium with inhibited carotenoid biosynthesis. Authors: Anna D Burtseva / Timur N Baymukhametov / Maxim A Bolshakov / Aleksandr S Starodubov / Huawei Zhang / Vladimir O Popov / Aleksandr A Ashikhmin / Konstantin M Boyko / ![]() Abstract: The LH2 complex is essential for light harvesting in many photosynthetic bacteria. To elucidate the specific structural role of carotenoids, we analyzed LH2 complexes from Ectothiorhodospira ...The LH2 complex is essential for light harvesting in many photosynthetic bacteria. To elucidate the specific structural role of carotenoids, we analyzed LH2 complexes from Ectothiorhodospira haloalkaliphila with inhibited carotenoid biosynthesis. This approach allowed us to study complexes incorporating the colorless carotenoid phytoene instead of the native, colored pigments. A 1.92 Å cryo-EM reconstruction revealed that phytoene fully substitutes for the native carotenoids while maintaining the octameric symmetry of the complex and the precise arrangement of bacteriochlorophylls. These results demonstrate that the architectural function of carotenoids in LH2 complexes is maintained even when their light-absorption capability is altered, providing new mechanistic insight into the structural basis of pigment-protein interactions in photosynthetic antenna complexes. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_65526.map.gz | 230.1 MB | EMDB map data format | |
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| Header (meta data) | emd-65526-v30.xml emd-65526.xml | 23.1 KB 23.1 KB | Display Display | EMDB header |
| Images | emd_65526.png | 77.7 KB | ||
| Filedesc metadata | emd-65526.cif.gz | 6.3 KB | ||
| Others | emd_65526_additional_1.map.gz emd_65526_half_map_1.map.gz emd_65526_half_map_2.map.gz | 117.3 MB 226.3 MB 226.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65526 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65526 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9w1cMC 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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Map
| File | Download / File: emd_65526.map.gz / Format: CCP4 / Size: 244.1 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: 0.67 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_65526_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_65526_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_65526_half_map_2.map | ||||||||||||
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Sample components
-Entire : LH2 complex from Ectothiorhodospira haloalkaliphila
| Entire | Name: LH2 complex from Ectothiorhodospira haloalkaliphila |
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| Components |
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-Supramolecule #1: LH2 complex from Ectothiorhodospira haloalkaliphila
| Supramolecule | Name: LH2 complex from Ectothiorhodospira haloalkaliphila / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) |
-Macromolecule #1: Light-harvesting protein B:800-850 subunit beta
| Macromolecule | Name: Light-harvesting protein B:800-850 subunit beta / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO |
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| Source (natural) | Organism: Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) |
| Molecular weight | Theoretical: 5.468237 KDa |
| Sequence | String: MYDNSISGLT EEQAKEFHEQ FKTTFTVFMV LAAAAHFLVF LWRPFY UniProtKB: Light-harvesting protein B:800-850 subunit beta |
-Macromolecule #2: Light-harvesting protein B-800/850 alpha chain
| Macromolecule | Name: Light-harvesting protein B-800/850 alpha chain / type: protein_or_peptide / ID: 2 / Number of copies: 8 / Enantiomer: LEVO |
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| Source (natural) | Organism: Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria) |
| Molecular weight | Theoretical: 7.855903 KDa |
| Sequence | String: MSEYRPSKPS NPRDDWKLWL VVNPGTWLMP ILMAVLVVAL VVHAFVYSND NYNPLTFDAS AEVAAEEAAE UniProtKB: Antenna complex alpha/beta subunit domain-containing protein |
-Macromolecule #3: BACTERIOCHLOROPHYLL A
| Macromolecule | Name: BACTERIOCHLOROPHYLL A / type: ligand / ID: 3 / Number of copies: 24 / Formula: BCL |
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| Molecular weight | Theoretical: 911.504 Da |
| Chemical component information | ![]() ChemComp-BCL: |
-Macromolecule #4: Phytoene
| Macromolecule | Name: Phytoene / type: ligand / ID: 4 / Number of copies: 8 / Formula: A1MBA |
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| Molecular weight | Theoretical: 544.936 Da |
-Macromolecule #5: water
| Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 88 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-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 R0.6/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Spherical aberration corrector: Microscope was modified with a Cs corrector (CEOS GmbH, Germany). Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 15 eV |
| Details | Preliminary grid screening was performed manually. |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 12334 / Average exposure time: 2.5 sec. / Average electron dose: 60.0 e/Å2 |
| 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: 0.01 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.6 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 |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9w1c: |
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About Yorodumi



Keywords
Ectothiorhodospira haloalkaliphila ATCC 51935 (bacteria)
Authors
Russian Federation, 1 items
Citation

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FIELD EMISSION GUN
