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Open data
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Basic information
| Entry | Database: PDB / ID: 6z5r | ||||||
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| Title | RC-LH1(16) complex from Rhodopseudomonas palustris | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / Reaction center / Light harvesting / Protein W / Quinone | ||||||
| Function / homology | Function and homology informationorganelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / metal ion binding / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | Rhodopseudomonas palustris (phototrophic) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | ||||||
Authors | Swainsbury, D.J.K. / Qian, P. / Hitchcock, A. / Hunter, C.N. | ||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Sci Adv / Year: 2021Title: Structures of RC-LH1 complexes with open or closed quinone channels. Authors: David J K Swainsbury / Pu Qian / Philip J Jackson / Kaitlyn M Faries / Dariusz M Niedzwiedzki / Elizabeth C Martin / David A Farmer / Lorna A Malone / Rebecca F Thompson / Neil A Ranson / ...Authors: David J K Swainsbury / Pu Qian / Philip J Jackson / Kaitlyn M Faries / Dariusz M Niedzwiedzki / Elizabeth C Martin / David A Farmer / Lorna A Malone / Rebecca F Thompson / Neil A Ranson / Daniel P Canniffe / Mark J Dickman / Dewey Holten / Christine Kirmaier / Andrew Hitchcock / C Neil Hunter / ![]() Abstract: The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes ...The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes from A 2.65-Å resolution structure of the RC-LH1-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC Q site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6z5r.cif.gz | 563.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6z5r.ent.gz | 485.2 KB | Display | PDB format |
| PDBx/mmJSON format | 6z5r.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6z5r_validation.pdf.gz | 5.6 MB | Display | wwPDB validaton report |
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| Full document | 6z5r_full_validation.pdf.gz | 5.8 MB | Display | |
| Data in XML | 6z5r_validation.xml.gz | 137.8 KB | Display | |
| Data in CIF | 6z5r_validation.cif.gz | 162.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z5/6z5r ftp://data.pdbj.org/pub/pdb/validation_reports/z5/6z5r | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 11080MC ![]() 6z5sC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
-Light-harvesting complex 1 ... , 2 types, 32 molecules CEGJNRTVPYA13579DFIKOSUXQZB24680
| #1: Protein/peptide | Mass: 5779.999 Da / Num. of mol.: 16 / Source method: isolated from a natural source Source: (natural) Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Strain: ATCC BAA-98 / CGA009 / References: UniProt: Q6N9L4 #2: Protein | Mass: 5849.797 Da / Num. of mol.: 16 / Source method: isolated from a natural source Source: (natural) Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Strain: ATCC BAA-98 / CGA009 / References: UniProt: Q6N9L5 |
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-Reaction center protein ... , 2 types, 2 molecules LM
| #4: Protein | Mass: 30857.777 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Strain: ATCC BAA-98 / CGA009 / References: UniProt: O83005 |
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| #5: Protein | Mass: 34453.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Strain: ATCC BAA-98 / CGA009 / References: UniProt: A0A4Z7 |
-Protein / Sugars , 2 types, 13 molecules H

| #10: Sugar | ChemComp-LMT / #3: Protein | | Mass: 27268.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Strain: ATCC BAA-98 / CGA009 / References: UniProt: A0A4Z9 |
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-Non-polymers , 10 types, 96 molecules 


















| #6: Chemical | ChemComp-BCL / #7: Chemical | ChemComp-CRT / #8: Chemical | ChemComp-6PL / ( #9: Chemical | ChemComp-CDL / #11: Chemical | #12: Chemical | ChemComp-U10 / #13: Chemical | ChemComp-FE / | #14: Chemical | ChemComp-QAK / ( | #15: Chemical | #16: Water | ChemComp-HOH / | |
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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: Reaction center-Light harvesting complex 1 / Type: COMPLEX Details: Reaction center-Light harvesting complex 1 from Rhodopseudomonas palustris Entity ID: #1-#5 / Source: NATURAL | ||||||||||||||||||||
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| Molecular weight | Value: 3.52 MDa / Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) (phototrophic)Cellular location: Lamellar membranes | ||||||||||||||||||||
| Buffer solution | pH: 8 | ||||||||||||||||||||
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was monodisperse | ||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 60 % / Chamber temperature: 298 K |
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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 |
| Image recording | Electron dose: 55.2 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 476547 / Details: Autopicked in RELION | |||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 260752 / Algorithm: FOURIER SPACE / Num. of class averages: 2 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: BACKBONE TRACE / Space: REAL | |||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Rhodopseudomonas palustris (phototrophic)
United Kingdom, 1items
Citation

UCSF Chimera






PDBj





