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- PDB-6mlu: Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2 -
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Open data
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Basic information
Entry | Database: PDB / ID: 6mlu | |||||||||||||||||||||
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Title | Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2 | |||||||||||||||||||||
![]() | Seipin | |||||||||||||||||||||
![]() | MEMBRANE PROTEIN / Lipid storage / Lipid droplet formation / lipodystrophy | |||||||||||||||||||||
Function / homology | ![]() positive regulation of axon extension involved in regeneration / diacylglycerol metabolic process / regulation of triglyceride metabolic process / lipid droplet formation / phosphatidic acid metabolic process / : / regulation of lipid storage / regulation of lipid biosynthetic process / positive regulation of lipid storage / lipid storage ...positive regulation of axon extension involved in regeneration / diacylglycerol metabolic process / regulation of triglyceride metabolic process / lipid droplet formation / phosphatidic acid metabolic process / : / regulation of lipid storage / regulation of lipid biosynthetic process / positive regulation of lipid storage / lipid storage / lipid droplet organization / endoplasmic reticulum calcium ion homeostasis / lipid biosynthetic process / fatty acid beta-oxidation / response to starvation / lipid droplet / endoplasmic reticulum membrane / endoplasmic reticulum Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | |||||||||||||||||||||
![]() | Sui, X. / Arlt, H. / Liao, M. / Walther, C.T. / Farese, V.R. | |||||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Cryo-electron microscopy structure of the lipid droplet-formation protein seipin. Authors: Xuewu Sui / Henning Arlt / Kelly P Brock / Zon Weng Lai / Frank DiMaio / Debora S Marks / Maofu Liao / Robert V Farese / Tobias C Walther / ![]() Abstract: Metabolic energy is stored in cells primarily as triacylglycerols in lipid droplets (LDs), and LD dysregulation leads to metabolic diseases. The formation of monolayer-bound LDs from the endoplasmic ...Metabolic energy is stored in cells primarily as triacylglycerols in lipid droplets (LDs), and LD dysregulation leads to metabolic diseases. The formation of monolayer-bound LDs from the endoplasmic reticulum (ER) bilayer is poorly understood, but the ER protein seipin is essential to this process. In this study, we report a cryo-electron microscopy structure and functional characterization of seipin. The structure reveals a ring-shaped dodecamer with the luminal domain of each monomer resolved at ∼4.0 Å. Each luminal domain monomer exhibits two distinctive features: a hydrophobic helix (HH) positioned toward the ER bilayer and a β-sandwich domain with structural similarity to lipid-binding proteins. This structure and our functional testing in cells suggest a model in which seipin oligomers initially detect forming LDs in the ER via HHs and subsequently act as membrane anchors to enable lipid transfer and LD growth. | |||||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.1 KB | Display | ![]() |
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PDB format | ![]() | 52.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 885.8 KB | Display | ![]() |
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Full document | ![]() | 887.5 KB | Display | |
Data in XML | ![]() | 20.8 KB | Display | |
Data in CIF | ![]() | 28.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9146MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 43957.070 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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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 |
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Sample preparation
Component | Name: cryo-EM protein structure of seipin/BSCL2 / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 43 kDa/nm / Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Protein sample was monodisperse. |
Vitrification | Instrument: GATAN CRYOPLUNGE 3 / Cryogen name: ETHANE / Humidity: 90 % |
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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: 58 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.12_2829: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: D12 (2x12 fold dihedral) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 22383 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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