+Open data
-Basic information
Entry | Database: PDB / ID: 8toh | ||||||
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Title | Cryo-EM structure of monomeric alpha-Klotho | ||||||
Components | Klotho | ||||||
Keywords | SIGNALING PROTEIN | ||||||
Function / homology | Function and homology information norepinephrine biosynthetic process / beta-glucuronidase / FGFR1c and Klotho ligand binding and activation / beta-glucuronidase activity / positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway / fibroblast growth factor receptor binding / vitamin D binding / energy reserve metabolic process / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 ...norepinephrine biosynthetic process / beta-glucuronidase / FGFR1c and Klotho ligand binding and activation / beta-glucuronidase activity / positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway / fibroblast growth factor receptor binding / vitamin D binding / energy reserve metabolic process / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 / response to vitamin D / negative regulation of systemic arterial blood pressure / response to angiotensin / beta-glucosidase activity / fibroblast growth factor binding / PI-3K cascade:FGFR1 / PI3K Cascade / fibroblast growth factor receptor signaling pathway / positive regulation of bone mineralization / calcium ion homeostasis / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR1 signaling / response to activity / determination of adult lifespan / Negative regulation of FGFR1 signaling / hormone activity / Constitutive Signaling by Aberrant PI3K in Cancer / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / carbohydrate metabolic process / apical plasma membrane / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.29 Å | ||||||
Authors | Schnicker, N.J. / Xu, Z. / Mohammad, A. / Gakhar, L. / Huang, C.L. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published Title: Exploring the a-Klotho conformational landscape Authors: Schnicker, N.J. / Xu, Z. / Mohammad, A. / Gakhar, L. / Huang, C.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8toh.cif.gz | 186.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8toh.ent.gz | 143.3 KB | Display | PDB format |
PDBx/mmJSON format | 8toh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/to/8toh ftp://data.pdbj.org/pub/pdb/validation_reports/to/8toh | HTTPS FTP |
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-Related structure data
Related structure data | 41452 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
#1: Protein | Mass: 109993.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KL / Cell line (production host): myeloma / Production host: Mus musculus (house mouse) / References: UniProt: Q9UEF7 |
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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: Human aKlotho / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||
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Molecular weight | Value: 0.13 MDa / Experimental value: YES | ||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||
Source (recombinant) | Organism: Mus musculus (house mouse) | ||||||||||||||||
Buffer solution | pH: 7.5 / Details: 25mM HEPES pH7.5, 300mM NaCl, 1mM TCEP | ||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 | ||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 279 K |
-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 magnification: 130000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm |
Specimen holder | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 1.099 sec. / Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 8676 |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 7891498 | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.29 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 115398 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | PDB-ID: 5w21 Pdb chain-ID: A / Accession code: 5w21 / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||
Refine LS restraints |
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