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Open data
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Basic information
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Title | Single particle structure of Atg18-WT | |||||||||
![]() | sharp map from CryoSPARC softwarew | |||||||||
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![]() | autophagy / membrane remodeling / PIP binding / PI3P / PI(3 / 5)P2 / lipid binding protein / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() regulation of phosphatidylinositol biosynthetic process / PAS complex / 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process / phagophore / positive regulation of vacuole organization / vacuolar protein processing / glycophagy / Macroautophagy / cytoplasm to vacuole targeting by the Cvt pathway / nucleophagy ...regulation of phosphatidylinositol biosynthetic process / PAS complex / 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process / phagophore / positive regulation of vacuole organization / vacuolar protein processing / glycophagy / Macroautophagy / cytoplasm to vacuole targeting by the Cvt pathway / nucleophagy / pexophagy / protein localization to phagophore assembly site / phagophore assembly site membrane / late endosome to vacuole transport / piecemeal microautophagy of the nucleus / phosphatidylinositol-3-phosphate binding / fungal-type vacuole membrane / phagophore assembly site / phosphatidylinositol-4-phosphate binding / phosphatidylinositol-3,5-bisphosphate binding / vacuolar membrane / extrinsic component of membrane / autophagosome assembly / ubiquitin binding / cell periphery / macroautophagy / endosome membrane / endosome / protein-containing complex / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.8 Å | |||||||||
![]() | Mann D / Fromm S / Martinez-Sanchez A / Gopaldass N / Mayer A / Sachse C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of Atg18 oligomers reveal a tilted structural scaffold for Atg2 at the isolation membrane Authors: Mann D / Fromm SA / Martinez-Sanchez A / Gopaldass N / Mayer A / Sachse C | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.3 KB 15.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.6 KB | Display | ![]() |
Images | ![]() | 86.1 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 59.3 MB 59.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 844.7 KB | Display | ![]() |
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Full document | ![]() | 844.2 KB | Display | |
Data in XML | ![]() | 16.2 KB | Display | |
Data in CIF | ![]() | 21 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8afxMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | sharp map from CryoSPARC softwarew | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8389 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: half map A
File | emd_15411_half_map_1.map | ||||||||||||
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Annotation | half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map B
File | emd_15411_half_map_2.map | ||||||||||||
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Annotation | half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Atg18
Entire | Name: Atg18 |
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Components |
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-Supramolecule #1: Atg18
Supramolecule | Name: Atg18 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Autophagy-related protein 18
Macromolecule | Name: Autophagy-related protein 18 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 54.62241 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SPTINFINFN QTGTCISLGT SKGFKIFNCE PFGKFYSEDS GGYAIVEMLF STSLLALVGI GDQPALSPRR LRIINTKKHS IICEVTFPT SILSVKMNKS RLVVLLQEQI YIYDINTMRL LHTIETNPNP RGLMAMSPSV ANSYLVYPSP PKVINSEIKA H ATTNNITL ...String: SPTINFINFN QTGTCISLGT SKGFKIFNCE PFGKFYSEDS GGYAIVEMLF STSLLALVGI GDQPALSPRR LRIINTKKHS IICEVTFPT SILSVKMNKS RLVVLLQEQI YIYDINTMRL LHTIETNPNP RGLMAMSPSV ANSYLVYPSP PKVINSEIKA H ATTNNITL SVGGNTETSF KRDQQDAGHS DISDLDQYSS FTKRDDADPT SSNGGNSSII KNGDVIVFNL ETLQPTMVIE AH KGEIAAM AISFDGTLMA TASDKGTIIR VFDIETGDKI YQFRRGTYAT RIYSISFSED SQYLAVTGSS KTVHIFKLGH SMS NNKLDS DDSNMEEAAA DDSSLDTTSI DALSDEENPT RLAREPYVDA SRKTMGRMIR YSSQKLSRRA ARTLGQIFPI KVTS LLESS RHFASLKLPV ETNSHVMTIS SIGSPIDIDT SEYPELFETG NSASTESYHE PVMKMVPIRV VSSDGYLYNF VMDPE RGGD CLILSQYSIL M UniProtKB: Autophagy-related protein 18 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS TALOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: COUNTING / Number real images: 5117 / Average electron dose: 70.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |