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- PDB-8zk2: Cryo-EM structure of photosynthetic LH1-RC core complex of Roseos... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8zk2 | ||||||
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Title | Cryo-EM structure of photosynthetic LH1-RC core complex of Roseospirillum parvum | ||||||
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![]() | PHOTOSYNTHESIS / LH1-RC core complex / ROSEOSPIRILLUM PARVUM 930I | ||||||
Function / homology | ![]() organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / electron transfer activity / iron ion binding / heme binding ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / electron transfer activity / iron ion binding / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.65 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 620.9 KB | Display | ![]() |
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PDB format | ![]() | 532.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 5 MB | Display | ![]() |
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Full document | ![]() | 5.2 MB | Display | |
Data in XML | ![]() | 140.8 KB | Display | |
Data in CIF | ![]() | 177.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 60165MC ![]() 8zjwC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Photosynthetic reaction center ... , 2 types, 2 molecules CH
#1: Protein | Mass: 39726.602 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#4: Protein | Mass: 27770.564 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Reaction center protein ... , 2 types, 2 molecules LM
#2: Protein | Mass: 30656.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#3: Protein | Mass: 35877.301 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 32 molecules BDFIKOQSUWYacegiAEGJNPRTVXZbdfhj
#5: Protein | Mass: 7382.300 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 7285.641 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Sugars , 1 types, 1 molecules 
#13: Sugar | ChemComp-LMT / |
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-Non-polymers , 9 types, 110 molecules 
















#7: Chemical | ChemComp-HEC / #8: Chemical | ChemComp-MG / #9: Chemical | ChemComp-PGV / ( #10: Chemical | ChemComp-8K6 / #11: Chemical | ChemComp-BCL / #12: Chemical | #14: Chemical | ChemComp-FE / | #15: Chemical | ChemComp-MQ8 / | #16: Chemical | ChemComp-CRT / |
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-Details
Has ligand of interest | Y |
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Has protein modification | Y |
-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-RC core complex / Type: COMPLEX / Entity ID: #1-#6 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() |
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: ![]() |
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: 2.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 281288 / Symmetry type: POINT | ||||||||||||||||||||||||
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