+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-7327 | |||||||||
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Title | CryoEM structure of mouse PCDH15-4EC-LHFPL5 complex | |||||||||
Map data | primary map | |||||||||
Sample |
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Function / homology | Function and homology information detection of mechanical stimulus involved in equilibrioception / equilibrioception / sensory perception of light stimulus / inner ear receptor cell stereocilium organization / righting reflex / detection of mechanical stimulus involved in sensory perception of sound / inner ear auditory receptor cell differentiation / stereocilium / non-motile cilium assembly / photoreceptor cell maintenance ...detection of mechanical stimulus involved in equilibrioception / equilibrioception / sensory perception of light stimulus / inner ear receptor cell stereocilium organization / righting reflex / detection of mechanical stimulus involved in sensory perception of sound / inner ear auditory receptor cell differentiation / stereocilium / non-motile cilium assembly / photoreceptor cell maintenance / adult walking behavior / auditory receptor cell stereocilium organization / startle response / homophilic cell adhesion via plasma membrane adhesion molecules / inner ear development / photoreceptor outer segment / visual perception / locomotory behavior / actin filament organization / morphogenesis of an epithelium / sensory perception of sound / multicellular organism growth / response to calcium ion / cell adhesion / synapse / calcium ion binding / extracellular space / membrane / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 11.33 Å | |||||||||
Authors | Gouaux E / Ge J / Elferich 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 | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_7327.map.gz | 78.2 MB | EMDB map data format | |
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Header (meta data) | emd-7327-v30.xml emd-7327.xml | 11.9 KB 11.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_7327_fsc.xml | 10.1 KB | Display | FSC data file |
Images | emd_7327.png | 53.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-7327 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-7327 | HTTPS FTP |
-Related structure data
Related structure data | 6c13MC 7328C 6c10C 6c14C C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_7327.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | primary map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.72 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Complex of membrane proteins
Entire | Name: Complex of membrane proteins |
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Components |
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-Supramolecule #1: Complex of membrane proteins
Supramolecule | Name: Complex of membrane proteins / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Mus musculus (house mouse) |
Recombinant expression | Organism: Homo sapiens (human) |
-Macromolecule #1: Protocadherin-15
Macromolecule | Name: Protocadherin-15 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 72.989023 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: QYDDSPVFTN STYTVVVEEN LPAGTSFLQI EAKDVDLGAN VSYRIRSPEV KHLFALHPFT GELSLLRSLD YEAFPDQEAS ITFLAEAFD IYGTMPPGIA TVTVIVKDMN DYPPVFSKRI YKGMVAPDAV KGTPITTVYA EDADPPGMPA SRVRYRVDDV Q FPYPASIF ...String: QYDDSPVFTN STYTVVVEEN LPAGTSFLQI EAKDVDLGAN VSYRIRSPEV KHLFALHPFT GELSLLRSLD YEAFPDQEAS ITFLAEAFD IYGTMPPGIA TVTVIVKDMN DYPPVFSKRI YKGMVAPDAV KGTPITTVYA EDADPPGMPA SRVRYRVDDV Q FPYPASIF DVEEDSGRVV TRVNLNEEPT TIFKLVVVAF DDGEPVMSSS ATVRILVLHP GEIPRFTQEE YRPPPVSELA AR GTVVGVI SAAAINQSIV YSIVAGNEED KFGINNVTGV IYVNSPLDYE TRTSYVLRVQ ADSLEVVLAN LRVPSKSNTA KVY IEIQDE NDHPPVFQKK FYIGGVSEDA RMFASVLRVK ATDRDTGNYS AMAYRLIIPP IKEGKEGFVV ETYTGLIKTA MLFH NMRRS YFKFQVIATD DYGKGLSGKA DVLVSVVNQL DMQVIVSNVP PTLVEKKIED LTEILDRYVQ EQIPGAKVVV ESIGA RRHG DAYSLEDYSK CDLTVYAIDP QTNRAIDRNE LFKFLDGKLL DINKDFQPYY GEGGRILEIR TPEAVTSIKK RGESLG YTE GALLALAFII ILCCIPAILV VLVSYRQFKV RQAECTKTAR IQSAMPAAKP AAPVPAAPAP PPPPPPPPPG AHLYEEL GE SAMHKYETAL FESRLVPR |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.5 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 285 K / Instrument: FEI VITROBOT MARK III |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Specialist optics | Phase plate: VOLTA PHASE PLATE |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 10.0 sec. / Average electron dose: 27.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Protocol: FLEXIBLE FIT |
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Output model | PDB-6c13: |