+Open data
-Basic information
Entry | Database: PDB / ID: 6du8 | ||||||
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Title | Human Polycsytin 2-l1 | ||||||
Components | Polycystic kidney disease 2-like 1 protein | ||||||
Keywords | MEMBRANE PROTEIN / polycystic 2-l1 / pc2l1 / pkd2l1 / TRPP2 | ||||||
Function / homology | Function and homology information sour taste receptor activity / detection of chemical stimulus involved in sensory perception of sour taste / sensory perception of sour taste / detection of chemical stimulus involved in sensory perception of taste / response to water / calcium-activated potassium channel activity / detection of mechanical stimulus / muscle alpha-actinin binding / cellular response to acidic pH / calcium-activated cation channel activity ...sour taste receptor activity / detection of chemical stimulus involved in sensory perception of sour taste / sensory perception of sour taste / detection of chemical stimulus involved in sensory perception of taste / response to water / calcium-activated potassium channel activity / detection of mechanical stimulus / muscle alpha-actinin binding / cellular response to acidic pH / calcium-activated cation channel activity / non-motile cilium / inorganic cation transmembrane transport / sodium channel activity / ciliary membrane / smoothened signaling pathway / alpha-actinin binding / monoatomic cation transport / sodium ion transmembrane transport / monoatomic cation channel activity / calcium channel complex / cytoskeletal protein binding / potassium ion transmembrane transport / calcium channel activity / actin cytoskeleton / cytoplasmic vesicle / protein homotetramerization / transmembrane transporter binding / receptor complex / intracellular membrane-bounded organelle / calcium ion binding / cell surface / endoplasmic reticulum / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.11 Å | ||||||
Authors | Hulse, R.E. / Clapham, D.E. / Li, Z. / Huang, R.K. / Zhang, J. | ||||||
Funding support | United States, 1items
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Citation | Journal: Elife / Year: 2018 Title: Cryo-EM structure of the polycystin 2-l1 ion channel. Authors: Raymond E Hulse / Zongli Li / Rick K Huang / Jin Zhang / David E Clapham / Abstract: We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation- ...We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6du8.cif.gz | 311.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6du8.ent.gz | 246.2 KB | Display | PDB format |
PDBx/mmJSON format | 6du8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6du8_validation.pdf.gz | 1015.5 KB | Display | wwPDB validaton report |
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Full document | 6du8_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 6du8_validation.xml.gz | 53.9 KB | Display | |
Data in CIF | 6du8_validation.cif.gz | 80.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/du/6du8 ftp://data.pdbj.org/pub/pdb/validation_reports/du/6du8 | HTTPS FTP |
-Related structure data
Related structure data | 8912MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 92070.633 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PKD2L1, PKD2L, PKDL, TRPP3 / Plasmid: pEG / Cell (production host): HEK-293S GnTl / Cell line (production host): HEK293S / Production host: Homo sapiens (human) / References: UniProt: Q9P0L9 #2: Sugar | ChemComp-NAG / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: 3D ARRAY / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Human polycystic 2-l / Type: ORGANELLE OR CELLULAR COMPONENT / Details: Homotetrameric assembly of polycystic 2-l1 / Entity ID: #1 / Source: RECOMBINANT | |||||||||||||||||||||||||
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Molecular weight | Value: 0.547 MDa / Experimental value: NO | |||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||
Source (recombinant) | Organism: Homo sapiens (human) / Plasmid: pEG | |||||||||||||||||||||||||
Buffer solution | pH: 7.5 | |||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 3.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: polycystic 2-l1 stabilized in amphipol PMAL-C8 | |||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 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: OTHER |
Electron lens | Mode: OTHER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.13_2998: / Classification: refinement |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C4 (4 fold cyclic) |
3D reconstruction | Resolution: 3.11 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 119334 / Num. of class averages: 8 / Symmetry type: POINT |