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Open data
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Basic information
Entry | Database: PDB / ID: 7zw1 | ||||||
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Title | Human PRPH2-ROM1 hetero-dimer | ||||||
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![]() | MEMBRANE PROTEIN / PRPH2 / peripherin-2 / ROM1 / hetero-complex / tetraspanin | ||||||
Function / homology | ![]() protein localization to photoreceptor outer segment / camera-type eye photoreceptor cell differentiation / response to low light intensity stimulus / photoreceptor cell outer segment organization / detection of light stimulus involved in visual perception / retina vasculature development in camera-type eye / protein heterooligomerization / photoreceptor outer segment membrane / plasma membrane => GO:0005886 / photoreceptor outer segment ...protein localization to photoreceptor outer segment / camera-type eye photoreceptor cell differentiation / response to low light intensity stimulus / photoreceptor cell outer segment organization / detection of light stimulus involved in visual perception / retina vasculature development in camera-type eye / protein heterooligomerization / photoreceptor outer segment membrane / plasma membrane => GO:0005886 / photoreceptor outer segment / visual perception / photoreceptor inner segment / protein homooligomerization / retina development in camera-type eye / regulation of gene expression / membrane => GO:0016020 / cell adhesion / protein homodimerization activity Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||
![]() | El Mazouni, D. / Gros, P. | ||||||
Funding support | European Union, 1items
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![]() | ![]() Title: Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis. Authors: Dounia El Mazouni / Piet Gros / ![]() Abstract: Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells ...Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells that enable vision. Here, we present single-particle cryo-electron microscopy structures of solubilized PRPH2-ROM1 heterodimers and higher-order oligomers. High-risk PRPH2 and ROM1 mutations causing blindness map to the protein-dimer interface. Cysteine bridges connect dimers forming positive-curved oligomers, whereas negative-curved oligomers were observed occasionally. Hexamers and octamers exhibit a secondary micelle that envelopes four carboxyl-terminal helices, supporting a potential role in membrane remodeling. Together, the data indicate multiple structures for PRPH2-ROM1 in creating and maintaining compartmentalization of photoreceptor cells. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 251.6 KB | Display | ![]() |
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PDB format | ![]() | 207.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 42.8 KB | Display | |
Data in CIF | ![]() | 61.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 14991MC 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: 40054.137 Da / Num. of mol.: 1 / Mutation: C150S Source method: isolated from a genetically manipulated source Details: HHHHHH = tag of purification Sequence of the protein starts at A-L-L (Aminoacids 2-3-4) Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 37249.828 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The protein sequence starts at A-P-V-L, residues 2-3-4-5 Source: (gene. exp.) ![]() ![]() |
#3: Antibody | Mass: 14646.134 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-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
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Molecular weight | Value: 76 kDa/nm / Experimental value: NO | ||||||||||||||||||||||||
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Buffer solution | pH: 7.6 | ||||||||||||||||||||||||
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 / Nominal defocus max: 2300 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.20.1_4487: / Classification: refinement | ||||||||||||||||||||||||
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EM software | Name: cryoSPARC / Version: 2.2 / Category: CTF correction | ||||||||||||||||||||||||
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 93727 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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