+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20673 | |||||||||
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Title | Cryo-EM Structure of Helical Lipoprotein Lipase | |||||||||
Map data | Helical Lipoprotein Lipase | |||||||||
Sample |
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Function / homology | Function and homology information Assembly of active LPL and LIPC lipase complexes / Chylomicron remodeling / Retinoid metabolism and transport / lipoprotein lipase / lipoprotein lipase activity / positive regulation of sequestering of triglyceride / low-density lipoprotein particle mediated signaling / chylomicron remodeling / positive regulation of cholesterol storage / phospholipase A1 ...Assembly of active LPL and LIPC lipase complexes / Chylomicron remodeling / Retinoid metabolism and transport / lipoprotein lipase / lipoprotein lipase activity / positive regulation of sequestering of triglyceride / low-density lipoprotein particle mediated signaling / chylomicron remodeling / positive regulation of cholesterol storage / phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / : / phospholipase A1 activity / triglyceride catabolic process / phospholipase activity / very-low-density lipoprotein particle remodeling / positive regulation of macrophage derived foam cell differentiation / chylomicron / high-density lipoprotein particle remodeling / cellular response to nutrient / very-low-density lipoprotein particle / triacylglycerol lipase activity / heparan sulfate proteoglycan binding / positive regulation of chemokine (C-X-C motif) ligand 2 production / triglyceride homeostasis / triglyceride metabolic process / cellular response to fatty acid / apolipoprotein binding / lipoprotein particle binding / catalytic complex / positive regulation of fat cell differentiation / phospholipid metabolic process / response to glucose / positive regulation of adipose tissue development / cholesterol homeostasis / positive regulation of interleukin-1 beta production / response to bacterium / positive regulation of interleukin-6 production / fatty acid biosynthetic process / positive regulation of inflammatory response / positive regulation of tumor necrosis factor production / heparin binding / signaling receptor binding / calcium ion binding / cell surface / protein homodimerization activity / extracellular space / plasma membrane Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) / Bovine (cattle) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
Authors | Gunn KH / Wang F / Egelman EH / Neher SB | |||||||||
Funding support | United States, 2 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2020 Title: The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage. Authors: Kathryn H Gunn / Benjamin S Roberts / Fengbin Wang / Joshua D Strauss / Mario J Borgnia / Edward H Egelman / Saskia B Neher / Abstract: Lipases are enzymes necessary for the proper distribution and utilization of lipids in the human body. Lipoprotein lipase (LPL) is active in capillaries, where it plays a crucial role in preventing ...Lipases are enzymes necessary for the proper distribution and utilization of lipids in the human body. Lipoprotein lipase (LPL) is active in capillaries, where it plays a crucial role in preventing dyslipidemia by hydrolyzing triglycerides from packaged lipoproteins. Thirty years ago, the existence of a condensed and inactive LPL oligomer was proposed. Although recent work has shed light on the structure of the LPL monomer, the inactive oligomer remained opaque. Here we present a cryo-EM reconstruction of a helical LPL oligomer at 3.8-Å resolution. Helix formation is concentration-dependent, and helices are composed of inactive dihedral LPL dimers. Heparin binding stabilizes LPL helices, and the presence of substrate triggers helix disassembly. Superresolution fluorescent microscopy of endogenous LPL revealed that LPL adopts a filament-like distribution in vesicles. Mutation of one of the helical LPL interaction interfaces causes loss of the filament-like distribution. Taken together, this suggests that LPL is condensed into its inactive helical form for storage in intracellular vesicles. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_20673.map.gz | 97.1 MB | EMDB map data format | |
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Header (meta data) | emd-20673-v30.xml emd-20673.xml | 14.2 KB 14.2 KB | Display Display | EMDB header |
Images | emd_20673.png | 323.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20673 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20673 | HTTPS FTP |
-Validation report
Summary document | emd_20673_validation.pdf.gz | 523.3 KB | Display | EMDB validaton report |
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Full document | emd_20673_full_validation.pdf.gz | 522.9 KB | Display | |
Data in XML | emd_20673_validation.xml.gz | 7 KB | Display | |
Data in CIF | emd_20673_validation.cif.gz | 7.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20673 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20673 | HTTPS FTP |
-Related structure data
Related structure data | 6u7mMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_20673.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Helical Lipoprotein Lipase | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.9317 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : filament of lipoprotein lipase
Entire | Name: filament of lipoprotein lipase |
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Components |
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-Supramolecule #1: filament of lipoprotein lipase
Supramolecule | Name: filament of lipoprotein lipase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Bos taurus (cattle) |
-Macromolecule #1: Lipoprotein lipase
Macromolecule | Name: Lipoprotein lipase / type: protein_or_peptide / ID: 1 / Number of copies: 30 / Enantiomer: LEVO / EC number: lipoprotein lipase |
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Source (natural) | Organism: Bovine (cattle) |
Molecular weight | Theoretical: 53.448789 KDa |
Sequence | String: MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTG MYESWVPKLV AALYKREPDS NVIVVDWLSR AQQHYPVSAG YTKLVGQDVA KFMNWMADEF NYPLGNVHLL G YSLGAHAA ...String: MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE DTAEDTCHLI PGVTESVANC HFNHSSKTFV VIHGWTVTG MYESWVPKLV AALYKREPDS NVIVVDWLSR AQQHYPVSAG YTKLVGQDVA KFMNWMADEF NYPLGNVHLL G YSLGAHAA GIAGSLTNKK VNRITGLDPA GPNFEYAEAP SRLSPDDADF VDVLHTFTRG SPGRSIGIQK PVGHVDIYPN GG TFQPGCN IGEALRVIAE RGLGDVDQLV KCSHERSVHL FIDSLLNEEN PSKAYRCNSK EAFEKGLCLS CRKNRCNNMG YEI NKVRAK RSSKMYLKTR SQMPYKVFHY QVKIHFSGTE SNTYTNQAFE ISLYGTVAES ENIPFTLPEV STNKTYSFLL YTEV DIGEL LMLKLKWISD SYFSWSNWWS SPGFDIGKIR VKAGETQKKV IFCSREKMSY LQKGKSPVIF VKCHDKSLNR KSG |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Concentration | 0.35 mg/mL | |||||||||||||||
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Buffer | pH: 8 Component:
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Grid | Pretreatment - Type: PLASMA CLEANING / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.038 kPa / Details: 15 mA current | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 98 % / Chamber temperature: 295 K / Instrument: LEICA EM GP / Details: Blot 3 seconds before plunging. |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number real images: 1764 / Average exposure time: 12.8 sec. / Average electron dose: 46.6 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 45000 |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |