+Open data
-Basic information
Entry | Database: PDB / ID: 3jac | ||||||
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Title | Cryo-EM study of a channel | ||||||
Components | Piezo-type mechanosensitive ion channel component 1 | ||||||
Keywords | METAL TRANSPORT / Cryo-EM / single particle | ||||||
Function / homology | Function and homology information mechanosensitive monoatomic cation channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / mechanosensitive monoatomic ion channel activity / positive regulation of integrin activation / positive regulation of myotube differentiation / monoatomic cation transport / lamellipodium membrane / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane ...mechanosensitive monoatomic cation channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / mechanosensitive monoatomic ion channel activity / positive regulation of integrin activation / positive regulation of myotube differentiation / monoatomic cation transport / lamellipodium membrane / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane / regulation of membrane potential / cellular response to mechanical stimulus / endoplasmic reticulum membrane / endoplasmic reticulum / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / negative staining / cryo EM / Resolution: 4.8 Å | ||||||
Authors | Ge, J. / Li, W. / Zhao, Q. / Li, N. / Xiao, B. / Gao, N. / Yang, M. | ||||||
Citation | Journal: Nature / Year: 2015 Title: Architecture of the mammalian mechanosensitive Piezo1 channel. Authors: Jingpeng Ge / Wanqiu Li / Qiancheng Zhao / Ningning Li / Maofei Chen / Peng Zhi / Ruochong Li / Ning Gao / Bailong Xiao / Maojun Yang / Abstract: Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have ...Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 Å. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore. | ||||||
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 | 3jac.cif.gz | 457 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3jac.ent.gz | 312.9 KB | Display | PDB format |
PDBx/mmJSON format | 3jac.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3jac_validation.pdf.gz | 888.1 KB | Display | wwPDB validaton report |
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Full document | 3jac_full_validation.pdf.gz | 1018.5 KB | Display | |
Data in XML | 3jac_validation.xml.gz | 73.4 KB | Display | |
Data in CIF | 3jac_validation.cif.gz | 116.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ja/3jac ftp://data.pdbj.org/pub/pdb/validation_reports/ja/3jac | HTTPS FTP |
-Related structure data
Related structure data | 6343MC 4raxC 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: 234834.109 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Piezo1, Fam38a / Production host: Homo sapiens (human) / References: UniProt: E2JF22 Sequence details | THE COMPLETE SEQUENCE OF THE PROTEIN IS BASED ON THE ENTIRE SEQUNCE OF UNIPROTKB E2JF22 (PIEZ1_ ...THE COMPLETE SEQUENCE OF THE PROTEIN IS BASED ON THE ENTIRE SEQUNCE OF UNIPROTKB E2JF22 (PIEZ1_MOUSE), WITH C-TERMINAL EXPRESSION | |
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