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Open data
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Basic information
Entry | Database: PDB / ID: 7q3e | |||||||||
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Title | Structure of the mouse CPLANE-RSG1 complex | |||||||||
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![]() | PROTEIN TRANSPORT / ciliogenesis / ciliopathies / longin / lipid binding | |||||||||
Function / homology | ![]() auditory receptor cell morphogenesis / axonemal basal plate / respiratory system development / tongue morphogenesis / regulation of embryonic cell shape / regulation of vesicle fusion / septin cytoskeleton organization / digestive system development / regulation of ruffle assembly / protein localization => GO:0008104 ...auditory receptor cell morphogenesis / axonemal basal plate / respiratory system development / tongue morphogenesis / regulation of embryonic cell shape / regulation of vesicle fusion / septin cytoskeleton organization / digestive system development / regulation of ruffle assembly / protein localization => GO:0008104 / regulation of fibroblast migration / podocyte cell migration / establishment of planar polarity / spinal cord dorsal/ventral patterning / motile cilium assembly / cilium organization / circulatory system development / Hedgehog 'off' state / negative regulation of cell division / positive regulation of cilium assembly / regulation of exocytosis / non-motile cilium assembly / regulation of smoothened signaling pathway / positive regulation of smoothened signaling pathway / camera-type eye development / motile cilium / regulation of establishment of cell polarity / neural tube development / limb development / regulation of focal adhesion assembly / smoothened signaling pathway / embryonic digit morphogenesis / hair follicle morphogenesis / roof of mouth development / exocytosis / axoneme / cilium assembly / regulation of ossification / negative regulation of keratinocyte proliferation / embryonic organ development / vesicle-mediated transport / keratinocyte differentiation / negative regulation of cell migration / ciliary basal body / kidney development / neural tube closure / establishment of protein localization / cilium / regulation of protein localization / protein transport / nervous system development / cytoskeleton / GTPase activity / GTP binding / cell surface / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.35 Å | |||||||||
![]() | Langousis, G. / Cavadini, S. / Kempf, G. / Matthias, P. | |||||||||
Funding support | 2items
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![]() | ![]() Title: Structure of the ciliogenesis-associated CPLANE complex. Authors: Gerasimos Langousis / Simone Cavadini / Niels Boegholm / Esben Lorentzen / Georg Kempf / Patrick Matthias / ![]() ![]() Abstract: Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ...Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ciliogenesis and planar polarity effector (CPLANE) proteins Wdpcp, Inturned, and Fuzzy. CPLANE proteins are essential for building the cilium and are mutated in multiple ciliopathies, yet their structure and molecular functions remain elusive. Here, we show that mammalian CPLANE proteins comprise a bona fide complex and report the near-atomic resolution structures of the human Wdpcp-Inturned-Fuzzy complex and of the mouse Wdpcp-Inturned-Fuzzy complex bound to the small guanosine triphosphatase Rsg1. Notably, the crescent-shaped CPLANE complex binds phospholipids such as phosphatidylinositol 3-phosphate via multiple modules and a CPLANE ciliopathy mutant exhibits aberrant lipid binding. Our study provides critical structural and functional insights into an enigmatic ciliogenesis-associated complex as well as unexpected molecular rationales for ciliopathies. | |||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 648.1 KB | Display | ![]() |
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PDB format | ![]() | 535.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 959.8 KB | Display | ![]() |
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Full document | ![]() | 961.6 KB | Display | |
Data in XML | ![]() | 47.7 KB | Display | |
Data in CIF | ![]() | 68.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 13790MC ![]() 7q3dC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 86286.477 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 107330.539 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Protein | Mass: 45542.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#4: Protein | Mass: 28459.801 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#5: Chemical | ChemComp-GTP / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: CPLANE complex / Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 1.04 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.35 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 94157 / Symmetry type: POINT |