+Open data
-Basic information
Entry | Database: PDB / ID: 7sc0 | ||||||
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Title | CryoEM structure of the Caveolin-1 8S complex | ||||||
Components | Caveolin-1 | ||||||
Keywords | STRUCTURAL PROTEIN / caveolin / caveolae / cryoEM / disc / monotopic proteins | ||||||
Function / homology | Function and homology information negative regulation of peptidyl-tyrosine autophosphorylation / : / caveolar macromolecular signaling complex / protein localization to plasma membrane raft / inward rectifier potassium channel inhibitor activity / negative regulation of inward rectifier potassium channel activity / : / regulation of peptidase activity / angiotensin-activated signaling pathway involved in heart process / caveola assembly ...negative regulation of peptidyl-tyrosine autophosphorylation / : / caveolar macromolecular signaling complex / protein localization to plasma membrane raft / inward rectifier potassium channel inhibitor activity / negative regulation of inward rectifier potassium channel activity / : / regulation of peptidase activity / angiotensin-activated signaling pathway involved in heart process / caveola assembly / intracellular nitric oxide homeostasis / protein localization to basolateral plasma membrane / negative regulation of protein tyrosine kinase activity / negative regulation of cytokine-mediated signaling pathway / insulin receptor internalization / cellular response to hyperoxia / regulation of entry of bacterium into host cell / positive regulation of toll-like receptor 3 signaling pathway / regulation of ruffle assembly / negative regulation of nitric-oxide synthase activity / regulation of cardiac muscle cell action potential involved in regulation of contraction / negative regulation of pinocytosis / regulation of membrane repolarization during action potential / negative regulation of potassium ion transmembrane transport / acrosomal membrane / regulation of the force of heart contraction by chemical signal / negative regulation of tyrosine phosphorylation of STAT protein / NOSTRIN mediated eNOS trafficking / FOXO-mediated transcription of cell cycle genes / mammary gland involution / positive regulation of cell adhesion molecule production / basement membrane organization / vesicle organization / maintenance of protein location in cell / patched binding / peptidase activator activity / regulation of fatty acid metabolic process / regulation of smooth muscle contraction / negative regulation of nitric oxide biosynthetic process / lipid storage / negative regulation of receptor signaling pathway via JAK-STAT / mammary gland development / regulation of ventricular cardiac muscle cell action potential / caveolin-mediated endocytosis / vasoconstriction / negative regulation of necroptotic process / cholesterol transport / RHOF GTPase cycle / RHOD GTPase cycle / positive regulation of extrinsic apoptotic signaling pathway / Disassembly of the destruction complex and recruitment of AXIN to the membrane / RND1 GTPase cycle / Basigin interactions / RND2 GTPase cycle / cellular response to peptide hormone stimulus / negative regulation of BMP signaling pathway / RND3 GTPase cycle / negative regulation of epithelial cell differentiation / positive regulation of cholesterol efflux / post-transcriptional regulation of gene expression / triglyceride metabolic process / negative regulation of MAPK cascade / positive regulation of catalytic activity / RHOB GTPase cycle / cholesterol binding / positive regulation of calcium ion transport into cytosol / cellular response to exogenous dsRNA / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / RHOC GTPase cycle / Triglyceride catabolism / RHOJ GTPase cycle / RHOQ GTPase cycle / plasma membrane => GO:0005886 / regulation of blood coagulation / regulation of heart rate by cardiac conduction / negative regulation of endothelial cell proliferation / negative regulation of peptidyl-serine phosphorylation / membrane depolarization / positive regulation of vasoconstriction / CDC42 GTPase cycle / positive regulation of gap junction assembly / RHOH GTPase cycle / negative regulation of anoikis / RHOG GTPase cycle / RHOA GTPase cycle / RAC2 GTPase cycle / RAC3 GTPase cycle / vasculogenesis / eNOS activation / calcium ion homeostasis / positive regulation of intrinsic apoptotic signaling pathway / skeletal muscle tissue development / negative regulation of MAP kinase activity / negative regulation of protein ubiquitination / cellular response to transforming growth factor beta stimulus / regulation of cytosolic calcium ion concentration / T cell costimulation / RAC1 GTPase cycle / lactation Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Porta, J.P. / Ohi, M.D. / Kenworthy, A.K. / Karakas, E. | ||||||
Funding support | United States, 1items
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Citation | Journal: Sci Adv / Year: 2022 Title: Molecular architecture of the human caveolin-1 complex. Authors: Jason C Porta / Bing Han / Alican Gulsevin / Jeong Min Chung / Yelena Peskova / Sarah Connolly / Hassane S Mchaourab / Jens Meiler / Erkan Karakas / Anne K Kenworthy / Melanie D Ohi / Abstract: Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin ...Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7sc0.cif.gz | 258.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7sc0.ent.gz | 210.9 KB | Display | PDB format |
PDBx/mmJSON format | 7sc0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7sc0_validation.pdf.gz | 924.2 KB | Display | wwPDB validaton report |
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Full document | 7sc0_full_validation.pdf.gz | 925.7 KB | Display | |
Data in XML | 7sc0_validation.xml.gz | 37.3 KB | Display | |
Data in CIF | 7sc0_validation.cif.gz | 62.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sc/7sc0 ftp://data.pdbj.org/pub/pdb/validation_reports/sc/7sc0 | HTTPS FTP |
-Related structure data
Related structure data | 25007MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 20494.576 Da / Num. of mol.: 11 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CAV1, CAV / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q03135 |
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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: Caveolin-1 8S complex with C11 symmetry. / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | |||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||
Source (recombinant) | Organism: Escherichia coli BL21 (bacteria) | |||||||||||||||||||||||||
Buffer solution | pH: 8 Details: Solutions were made fresh for each preparation of 8S particles | |||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 1.1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Specimen support | Details: 5 mA glow discharge / Grid material: GOLD / 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: 293 K |
-Electron microscopy imaging
Microscopy | Model: TFS GLACIOS |
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Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 36000 X / Calibrated magnification: 40103 X / Nominal defocus max: 2200 nm / Nominal defocus min: 1500 nm / Calibrated defocus min: 1500 nm / Calibrated defocus max: 2200 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm / Alignment procedure: BASIC |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: OTHER |
Image recording | Average exposure time: 6 sec. / Electron dose: 55.5 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 984 |
Image scans | Sampling size: 0.98 µm / Width: 3838 / Height: 3710 / Movie frames/image: 30 / Used frames/image: 1-30 |
-Processing
Software | Name: PHENIX / Version: 1.19.1_4122: / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 394900 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C11 (11 fold cyclic) | ||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 60615 / Algorithm: BACK PROJECTION / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | B value: 37.8 / Protocol: AB INITIO MODEL / Space: REAL / Target criteria: Correlation coefficient | ||||||||||||||||||||||||||||||||||||||||||||||||||
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