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- EMDB-60158: Cryo-EM structure of photosynthetic LH1' complex of Roseospirillu... -
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Open data
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Basic information
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Title | Cryo-EM structure of photosynthetic LH1' complex of Roseospirillum parvum | |||||||||
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![]() | LH1 prime complex / ROSEOSPIRILLUM PARVUM 930I / PHOTOSYNTHESIS | |||||||||
Function / homology | ![]() organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / : / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.35 Å | |||||||||
![]() | Wang G-L / Wang X-P / Yu L-J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum. Authors: Xiang-Ping Wang / Guang-Lei Wang / Yuan Fu / Akane Minamino / Mei-Juan Zou / Fei Ma / Bo Xu / Zheng-Yu Wang-Otomo / Yukihiro Kimura / Michael T Madigan / Jörg Overmann / Long-Jiang Yu / ![]() ![]() ![]() ![]() Abstract: Purple phototrophic bacteria produce two kinds of light-harvesting complexes that function to capture and transmit solar energy: the core antenna (LH1) and the peripheral antenna (LH2). The ...Purple phototrophic bacteria produce two kinds of light-harvesting complexes that function to capture and transmit solar energy: the core antenna (LH1) and the peripheral antenna (LH2). The apoproteins of these antennas, encoded respectively by the genes pufBA and pucBA within and outside the photosynthetic gene cluster, respectively, exhibit conserved amino acid sequences and structural topologies suggesting they were derived from a shared ancestor. Here we present the structures of two photosynthetic complexes from Roseospirillum (Rss.) parvum 930I: an LH1-RC complex and a variant of the LH1 complex also encoded by pufBA that we designate as LH1'. The LH1-RC complex forms a closed elliptical structure consisting of 16 pairs of αβ-polypeptides that surrounds the RC. By contrast, the LH1' complex is a closed ring structure composed of 14 pairs of αβ-polypeptides, and it shows significant similarities to LH2 complexes both spectrally and structurally. Although LH2-like, the LH1' complex is larger than any known LH2 complexes, and genomic analyses of Rss. parvum revealed the absence of pucBA, genes that encode classical LH2 complexes. Characterization of the unique Rss. parvum photocomplexes not only underscores the diversity of such structures but also sheds new light on the evolution of light-harvesting complexes from phototrophic bacteria. | |||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 168 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.7 KB 14.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.7 KB | Display | ![]() |
Images | ![]() | 57.8 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Others | ![]() ![]() | 164.3 MB 164.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8zjwMC ![]() 8zk2C 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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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_60158_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_60158_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : LH1 prime complex
Entire | Name: LH1 prime complex |
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Components |
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-Supramolecule #1: LH1 prime complex
Supramolecule | Name: LH1 prime complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Beta subunit of light-harvesting 1 complex
Macromolecule | Name: Beta subunit of light-harvesting 1 complex / type: protein_or_peptide / ID: 1 / Number of copies: 14 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 7.3823 KDa |
Sequence | String: MATTENVTSS TGLTEAEAKE FHAVYSQSAA GFLAVCAVAH VLAWMWRPFW PGAEGWVMDT AQNLTFLA UniProtKB: Beta subunit of light-harvesting 1 complex |
-Macromolecule #2: Alpha subunit of light-harvesting 1 complex
Macromolecule | Name: Alpha subunit of light-harvesting 1 complex / type: protein_or_peptide / ID: 2 / Number of copies: 14 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 7.285641 KDa |
Sequence | String: MTFSTHKVWL MFDPRSTLVA LAAFLVVLAL LIHFLCLGHD RFNWLEGNPA ATKAAAAAVT MPVNPVA UniProtKB: Alpha subunit of light-harvesting 1 complex |
-Macromolecule #3: BACTERIOCHLOROPHYLL A
Macromolecule | Name: BACTERIOCHLOROPHYLL A / type: ligand / ID: 3 / Number of copies: 42 / Formula: BCL |
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Molecular weight | Theoretical: 911.504 Da |
Chemical component information | ![]() ChemComp-BCL: |
-Macromolecule #4: SPIRILLOXANTHIN
Macromolecule | Name: SPIRILLOXANTHIN / type: ligand / ID: 4 / Number of copies: 14 / Formula: CRT |
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Molecular weight | Theoretical: 596.925 Da |
Chemical component information | ![]() ChemComp-CRT: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
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 TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 61.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |