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Yorodumi- PDB-8b64: Cryo-EM structure of RC-LH1-PufX photosynthetic core complex from... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8b64 | ||||||
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Title | Cryo-EM structure of RC-LH1-PufX photosynthetic core complex from Rba. capsulatus | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / PufX / core complex / RC-LH1 / Rba capsulatus / photosynthetic core | ||||||
Function / homology | Function and homology information 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 transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthesis / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Rhodobacter capsulatus (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.589 Å | ||||||
Authors | Bracun, L. / Yamagata, A. / Shirouzu, M. / Liu, L.N. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Structure / Year: 2023 Title: Cryo-EM structure of a monomeric RC-LH1-PufX supercomplex with high-carotenoid content from Rhodobacter capsulatus. Authors: Laura Bracun / Atsushi Yamagata / Bern M Christianson / Mikako Shirouzu / Lu-Ning Liu / Abstract: In purple photosynthetic bacteria, the photochemical reaction center (RC) and light-harvesting complex 1 (LH1) assemble to form monomeric or dimeric RC-LH1 membrane complexes, essential for bacterial ...In purple photosynthetic bacteria, the photochemical reaction center (RC) and light-harvesting complex 1 (LH1) assemble to form monomeric or dimeric RC-LH1 membrane complexes, essential for bacterial photosynthesis. Here, we report a 2.59-Å resolution cryoelectron microscopy (cryo-EM) structure of the RC-LH1 supercomplex from Rhodobacter capsulatus. We show that Rba. capsulatus RC-LH1 complexes are exclusively monomers in which the RC is surrounded by a 15-subunit LH1 ring. Incorporation of a transmembrane polypeptide PufX leads to a large opening within the LH1 ring. Each LH1 subunit associates two carotenoids and two bacteriochlorophylls, which is similar to Rba. sphaeroides RC-LH1 but more than one carotenoid per LH1 in Rba. veldkampii RC-LH1 monomer. Collectively, the unique Rba. capsulatus RC-LH1-PufX represents an intermediate structure between Rba. sphaeroides and Rba. veldkampii RC-LH1-PufX. Comparison of PufX from the three Rhodobacter species indicates the important residues involved in dimerization of RC-LH1. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8b64.cif.gz | 613 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8b64.ent.gz | 454.6 KB | Display | PDB format |
PDBx/mmJSON format | 8b64.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b6/8b64 ftp://data.pdbj.org/pub/pdb/validation_reports/b6/8b64 | HTTPS FTP |
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-Related structure data
Related structure data | 15862MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 2 types, 16 molecules aebdtsuronkjigfX
#1: Protein | Mass: 6600.920 Da / Num. of mol.: 15 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P02948 #3: Protein | | Mass: 8574.901 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P26240 |
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-Protein/peptide , 1 types, 15 molecules DAEBSTUORKNIJFG
#2: Protein/peptide | Mass: 5470.303 Da / Num. of mol.: 15 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P02950 |
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-Reaction center protein ... , 3 types, 3 molecules LMH
#4: Protein | Mass: 31586.795 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P19057 |
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#5: Protein | Mass: 34462.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P11847 |
#6: Protein | Mass: 28569.580 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / References: UniProt: P19056 |
-Non-polymers , 6 types, 75 molecules
#7: Chemical | ChemComp-BCL / #8: Chemical | ChemComp-SPO / #9: Chemical | #10: Chemical | ChemComp-U10 / #11: Chemical | ChemComp-3PE / #12: Chemical | ChemComp-FE / | |
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-Details
Has ligand of interest | Y |
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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 |
-Sample preparation
Component | Name: RC-LH1-PufX photosynthetic core complex from Rba. capsulatus Type: COMPLEX / Entity ID: #1-#6 / Source: NATURAL |
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Source (natural) | Organism: Rhodobacter capsulatus (bacteria) / Strain: SB1003 |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE |
-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 FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 50.32 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
Software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.589 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 181054 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.23 Å2 | ||||||||||||||||||||||||
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