+Open data
-Basic information
Entry | Database: PDB / ID: 6c14 | ||||||
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Title | CryoEM structure of mouse PCDH15-1EC-LHFPL5 complex | ||||||
Components |
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Keywords | membrane protein / metal transport / PCDH15 / LHFPL5 / protocadherin / tip link / hair cell / TMHS / hearing | ||||||
Function / homology | Function and homology information detection of mechanical stimulus involved in equilibrioception / detection of mechanical stimulus involved in sensory perception of sound / detection of mechanical stimulus involved in sensory perception / inner ear receptor cell stereocilium organization / stereocilium tip / righting reflex / stereocilium bundle / inner ear auditory receptor cell differentiation / stereocilium / non-motile cilium assembly ...detection of mechanical stimulus involved in equilibrioception / detection of mechanical stimulus involved in sensory perception of sound / detection of mechanical stimulus involved in sensory perception / inner ear receptor cell stereocilium organization / stereocilium tip / righting reflex / stereocilium bundle / inner ear auditory receptor cell differentiation / stereocilium / non-motile cilium assembly / auditory receptor cell stereocilium organization / adult walking behavior / homophilic cell adhesion via plasma membrane adhesion molecules / startle response / inner ear development / photoreceptor outer segment / monoatomic ion transport / visual perception / actin filament organization / morphogenesis of an epithelium / locomotory behavior / sensory perception of sound / multicellular organism growth / response to calcium ion / cell adhesion / apical plasma membrane / calcium ion binding / extracellular region / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.5 Å | ||||||
Authors | Gouaux, E. / Elferich, J. / Ge, J. | ||||||
Citation | Journal: Elife / Year: 2018 Title: Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. Authors: Jingpeng Ge / Johannes Elferich / April Goehring / Huaying Zhao / Peter Schuck / Eric Gouaux / Abstract: Hearing and balance involve the transduction of mechanical stimuli into electrical signals by deflection of bundles of stereocilia linked together by protocadherin 15 (PCDH15) and cadherin 23 'tip ...Hearing and balance involve the transduction of mechanical stimuli into electrical signals by deflection of bundles of stereocilia linked together by protocadherin 15 (PCDH15) and cadherin 23 'tip links'. PCDH15 transduces tip link tension into opening of a mechano-electrical transduction (MET) ion channel. PCDH15 also interacts with LHFPL5, a candidate subunit of the MET channel. Here we illuminate the PCDH15-LHFPL5 structure, showing how the complex is composed of PCDH15 and LHFPL5 subunit pairs related by a 2-fold axis. The extracellular cadherin domains define a mobile tether coupled to a rigid, 2-fold symmetric 'collar' proximal to the membrane bilayer. LHFPL5 forms extensive interactions with the PCDH15 transmembrane helices and stabilizes the overall PCDH15-LHFPL5 assembly. Our studies illuminate the architecture of the PCDH15-LHFPL5 complex, localize mutations associated with deafness, and shed new light on how forces in the PCDH15 tether may be transduced into the stereocilia membrane. | ||||||
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 | 6c14.cif.gz | 197.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6c14.ent.gz | 157.3 KB | Display | PDB format |
PDBx/mmJSON format | 6c14.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6c14_validation.pdf.gz | 909.9 KB | Display | wwPDB validaton report |
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Full document | 6c14_full_validation.pdf.gz | 914.5 KB | Display | |
Data in XML | 6c14_validation.xml.gz | 34.9 KB | Display | |
Data in CIF | 6c14_validation.cif.gz | 51.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c1/6c14 ftp://data.pdbj.org/pub/pdb/validation_reports/c1/6c14 | HTTPS FTP |
-Related structure data
Related structure data | 7328MC 7327C 6c10C 6c13C 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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-Components
#1: Protein | Mass: 37458.129 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Pcdh15 / Production host: Homo sapiens (human) / References: UniProt: Q99PJ1 #2: Protein | Mass: 25067.320 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Lhfpl5, Tmhs / Production host: Homo sapiens (human) / References: UniProt: Q4KL25 |
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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: membrane protein complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||||||
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Source (natural) | Organism: Mus musculus (house mouse) | ||||||||||||||||||||
Source (recombinant) | Organism: Homo sapiens (human) | ||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 285 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 |
Image recording | Electron dose: 74 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.12_2829: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 78792 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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