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Open data
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Basic information
| Entry | Database: PDB / ID: 9kll | ||||||||||||||||||||||||||||||||||||
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| Title | Striga MAX2-ASK1 complex | ||||||||||||||||||||||||||||||||||||
Components |
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Keywords | SIGNALING PROTEIN / Strigolactone / SCF / Ubiquitination | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationphragmoplast / jasmonic acid mediated signaling pathway / ethylene-activated signaling pathway / response to jasmonic acid / response to auxin / auxin-activated signaling pathway / negative regulation of DNA recombination / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / chromosome segregation ...phragmoplast / jasmonic acid mediated signaling pathway / ethylene-activated signaling pathway / response to jasmonic acid / response to auxin / auxin-activated signaling pathway / negative regulation of DNA recombination / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / chromosome segregation / microtubule cytoskeleton organization / spindle / ubiquitin-dependent protein catabolic process / protein ubiquitination / mitochondrion / nucleus / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | ![]() Striga hermonthica (purple witchweed) | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | ||||||||||||||||||||||||||||||||||||
Authors | Vancea, A.I. / Huntington, B. / Savva, C.G. / Arold, S.T. | ||||||||||||||||||||||||||||||||||||
| Funding support | Saudi Arabia, 1items
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Citation | Journal: To Be PublishedTitle: Mechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase-receptor-substrate complex Authors: Vancea, A.I. / Huntington, B. / Steinchen, W. / Savva, C.G. / Hameed, U.F.S. / Arold, S.T. | ||||||||||||||||||||||||||||||||||||
| History |
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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 | 9kll.cif.gz | 165.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kll.ent.gz | 125.6 KB | Display | PDB format |
| PDBx/mmJSON format | 9kll.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kl/9kll ftp://data.pdbj.org/pub/pdb/validation_reports/kl/9kll | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 62408MC ![]() 9kkxC ![]() 9kldC ![]() 9klkC ![]() 9klvC C: citing same article ( M: map data used to model this data |
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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: 17876.043 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Protein | Mass: 85626.188 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: N-terminal 9xHis and Strep-tag / Source: (gene. exp.) Striga hermonthica (purple witchweed) / Gene: MAX2 / Plasmid: pACEBac1 / Production host: ![]() |
| Has protein modification | N |
-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
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
| Buffer component |
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| Specimen | Conc.: 0.35 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Specimen support | Details: 30 mA / Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R1.2/1.3 | ||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 165000 X / Nominal defocus max: 2700 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 90 K / Temperature (min): 80 K |
| Image recording | Average exposure time: 3 sec. / Electron dose: 44 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 20175 |
| EM imaging optics | Energyfilter name: TFS Selectris X / Energyfilter slit width: 10 eV |
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Processing
| EM software | Name: PHENIX / Version: 1.21_5207: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 524247 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||
| Atomic model building |
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| Refine LS restraints |
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About Yorodumi






Saudi Arabia, 1items
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