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Yorodumi- PDB-8zjw: Cryo-EM structure of photosynthetic LH1' complex of Roseospirillu... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8zjw | ||||||
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| Title | Cryo-EM structure of photosynthetic LH1' complex of Roseospirillum parvum | ||||||
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Keywords | PHOTOSYNTHESIS / LH1 prime complex / ROSEOSPIRILLUM PARVUM 930I | ||||||
| Function / homology | Function and homology informationorganelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / metal ion binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Roseospirillum parvum (bacteria) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.35 Å | ||||||
Authors | Wang, G.-L. / Wang, X.-P. / Yu, L.-J. | ||||||
| Funding support | China, 1items
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Citation | Journal: Commun Biol / Year: 2024Title: 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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8zjw.cif.gz | 339 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8zjw.ent.gz | 296.1 KB | Display | PDB format |
| PDBx/mmJSON format | 8zjw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zj/8zjw ftp://data.pdbj.org/pub/pdb/validation_reports/zj/8zjw | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 60158MC ![]() 8zk2C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 7382.300 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Source: (natural) Roseospirillum parvum (bacteria) / References: UniProt: Q6XBJ9#2: Protein | Mass: 7285.641 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Source: (natural) Roseospirillum parvum (bacteria) / References: UniProt: Q6XBJ8#3: Chemical | ChemComp-BCL / #4: Chemical | ChemComp-CRT / Has ligand of interest | Y | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: LH1 prime complex / Type: COMPLEX / Entity ID: #1-#2 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Roseospirillum parvum (bacteria) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2400 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 61.6 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.35 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 397127 / Symmetry type: POINT | ||||||||||||||||||||||||
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Roseospirillum parvum (bacteria)
China, 1items
Citation




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FIELD EMISSION GUN