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- EMDB-36907: Cryo-EM structure of the RC-LH core comples from Halorhodospira h... -
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Basic information
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Title | Cryo-EM structure of the RC-LH core comples from Halorhodospira halochloris | |||||||||
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![]() | RC-LH complex / HALORHODOSPIRA HALOCHLORIS / ![]() | |||||||||
Function / homology | ![]() organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Wang G-L / Qi C-H / Yu L-J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the unusual core photocomplex from a triply extremophilic purple bacterium, Halorhodospira halochloris. Authors: Chen-Hui Qi / Guang-Lei Wang / Fang-Fang Wang / Jie Wang / Xiang-Ping Wang / Mei-Juan Zou / Fei Ma / Michael T Madigan / Yukihiro Kimura / Zheng-Yu Wang-Otomo / Long-Jiang Yu / ![]() ![]() ![]() Abstract: Halorhodospira (Hlr.) halochloris is a triply extremophilic phototrophic purple sulfur bacterium, as it is thermophilic, alkaliphilic, and extremely halophilic. The light-harvesting-reaction center ...Halorhodospira (Hlr.) halochloris is a triply extremophilic phototrophic purple sulfur bacterium, as it is thermophilic, alkaliphilic, and extremely halophilic. The light-harvesting-reaction center (LH1-RC) core complex of this bacterium displays an LH1-Q transition at 1,016 nm, which is the lowest-energy wavelength absorption among all known phototrophs. Here we report the cryo-EM structure of the LH1-RC at 2.42 Å resolution. The LH1 complex forms a tricyclic ring structure composed of 16 αβγ-polypeptides and one αβ-heterodimer around the RC. From the cryo-EM density map, two previously unrecognized integral membrane proteins, referred to as protein G and protein Q, were identified. Both of these proteins are single transmembrane-spanning helices located between the LH1 ring and the RC L-subunit and are absent from the LH1-RC complexes of all other purple bacteria of which the structures have been determined so far. Besides bacteriochlorophyll b molecules (B1020) located on the periplasmic side of the Hlr. halochloris membrane, there are also two arrays of bacteriochlorophyll b molecules (B800 and B820) located on the cytoplasmic side. Only a single copy of a carotenoid (lycopene) was resolved in the Hlr. halochloris LH1-α3β3 and this was positioned within the complex. The potential quinone channel should be the space between the LH1-α3β3 that accommodates the single lycopene but does not contain a γ-polypeptide, B800 and B820. Our results provide a structural explanation for the unusual Q red shift and carotenoid absorption in the Hlr. halochloris spectrum and reveal new insights into photosynthetic mechanisms employed by a species that thrives under the harshest conditions of any phototrophic microorganism known. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 167.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 27.8 KB 27.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.3 KB | Display | ![]() |
Images | ![]() | 53.1 KB | ||
Filedesc metadata | ![]() | 7.8 KB | ||
Others | ![]() ![]() | 165.5 MB 165.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8k5oMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.02 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
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Projections & Slices |
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
+Entire : RC-LH core complex
+Supramolecule #1: RC-LH core complex
+Macromolecule #1: Photosynthetic reaction center cytochrome c subunit
+Macromolecule #2: Reaction center protein L chain
+Macromolecule #3: Reaction center protein M chain
+Macromolecule #4: Photosynthetic reaction center H subunit
+Macromolecule #5: Antenna complex alpha/beta subunit domain-containing protein
+Macromolecule #6: Light-harvesting LHI
+Macromolecule #7: Antenna complex alpha/beta subunit domain-containing protein
+Macromolecule #8: Beta subunit of light-harvesting 1
+Macromolecule #9: Gamma subunit of light-harvesting 1
+Macromolecule #10: reaction center small polypeptide
+Macromolecule #11: reactin center small polypeptide
+Macromolecule #12: HEME C
+Macromolecule #13: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...
+Macromolecule #14: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
+Macromolecule #15: Trans-Geranyl Bacteriochlorophyll B
+Macromolecule #16: Trans-Geranyl Bacteriopheophytin B
+Macromolecule #17: Ubiquinone-8
+Macromolecule #18: UNKNOWN LIGAND
+Macromolecule #19: FE (III) ION
+Macromolecule #20: MENAQUINONE 8
+Macromolecule #21: CARDIOLIPIN
+Macromolecule #22: LYCOPENE
+Macromolecule #23: Trans-Geranyl 8-vinyl-bacteriochlorophyll B
+Macromolecule #24: DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE
+Macromolecule #25: 2-O-octyl-beta-D-glucopyranose
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 60.8 e/Å2 |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |