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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Cryo-EM structure of human ATG2A-WIPI4 complex | |||||||||
![]() | Half map A of ATG2A-WIPI4 complex | |||||||||
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![]() | Lipid transport / ATG2A-WIPI4 complex / single particle cryo-EM / Peripheral membrane proteins / LIPID TRANSPORT-MEMBRANE PROTEIN complex | |||||||||
Function / homology | ![]() phagophore / lipid transfer activity / organelle membrane contact site / glycophagy / phosphatidylinositol phosphate binding / nucleophagy / positive regulation of autophagosome assembly / protein localization to phagophore assembly site / phagophore assembly site membrane / piecemeal microautophagy of the nucleus ...phagophore / lipid transfer activity / organelle membrane contact site / glycophagy / phosphatidylinositol phosphate binding / nucleophagy / positive regulation of autophagosome assembly / protein localization to phagophore assembly site / phagophore assembly site membrane / piecemeal microautophagy of the nucleus / phosphatidylinositol-3-phosphate binding / phagophore assembly site / phosphatidylinositol-3,5-bisphosphate binding / reticulophagy / extrinsic component of membrane / Macroautophagy / autophagosome assembly / protein-membrane adaptor activity / cellular response to starvation / lipid droplet / autophagy / endoplasmic reticulum membrane / protein kinase binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.23 Å | |||||||||
![]() | Wang Y / Stjepanovic G | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for lipid transfer by the ATG2A-ATG9A complex Authors: Wang Y / Stjepanovic G | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 483.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.4 KB 16.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17 KB | Display | ![]() |
Images | ![]() | 82.9 KB | ||
Filedesc metadata | ![]() | 6.8 KB | ||
Others | ![]() ![]() | 475.8 MB 475.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 757.7 KB | Display | ![]() |
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Full document | ![]() | 757.3 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 34.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8kbxMC ![]() 8kbyC ![]() 8kbzC ![]() 8kc3C C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Half map A of ATG2A-WIPI4 complex | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map B of ATG2A-WIPI4 complex
File | emd_37086_half_map_1.map | ||||||||||||
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Annotation | Half map B of ATG2A-WIPI4 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B of ATG2A-WIPI4 complex
File | emd_37086_half_map_2.map | ||||||||||||
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Annotation | Half map B of ATG2A-WIPI4 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : ATG2A-WIPI4 complex
Entire | Name: ATG2A-WIPI4 complex |
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Components |
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-Supramolecule #1: ATG2A-WIPI4 complex
Supramolecule | Name: ATG2A-WIPI4 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 253 KDa |
-Macromolecule #1: WD repeat domain phosphoinositide-interacting protein 4
Macromolecule | Name: WD repeat domain phosphoinositide-interacting protein 4 type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 39.916539 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MTQQPLRGVT SLRFNQDQSC FCCAMETGVR IYNVEPLMEK GHLDHEQVGS MGLVEMLHRS NLLALVGGGS SPKFSEISVL IWDDAREGK DSKEKLVLEF TFTKPVLSVR MRHDKIVIVL KNRIYVYSFP DNPRKLFEFD TRDNPKGLCD LCPSLEKQLL V FPGHKCGS ...String: MTQQPLRGVT SLRFNQDQSC FCCAMETGVR IYNVEPLMEK GHLDHEQVGS MGLVEMLHRS NLLALVGGGS SPKFSEISVL IWDDAREGK DSKEKLVLEF TFTKPVLSVR MRHDKIVIVL KNRIYVYSFP DNPRKLFEFD TRDNPKGLCD LCPSLEKQLL V FPGHKCGS LQLVDLASTK PGTSSAPFTI NAHQSDIACV SLNQPGTVVA SASQKGTLIR LFDTQSKEKL VELRRGTDPA TL YCINFSH DSSFLCASSD KGTVHIFALK DTRLNRRSAL ARVGKVGPMI GQYVDSQWSL ASFTVPAESA CICAFGRNTS KNV NSVIAI CVDGTFHKYV FTPDGNCNRE AFDVYLDICD DDDF UniProtKB: WD repeat domain phosphoinositide-interacting protein 4 |
-Macromolecule #2: Autophagy-related protein 2 homolog A
Macromolecule | Name: Autophagy-related protein 2 homolog A / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 213.100281 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSRWLWPWSN CVKERVCRYL LHHYLGHFFQ EHLSLDQLSL DLYKGSVALR DIHLEIWSVN EVLESMESPL ELVEGFVGSI EVAVPWAAL LTDHCTVRVS GLQLTLQPRR GPAPGAADSQ SWASCMTTSL QLAQECLRDG LPEPSEPPQP LEGLEMFAQT I ETVLRRIK ...String: MSRWLWPWSN CVKERVCRYL LHHYLGHFFQ EHLSLDQLSL DLYKGSVALR DIHLEIWSVN EVLESMESPL ELVEGFVGSI EVAVPWAAL LTDHCTVRVS GLQLTLQPRR GPAPGAADSQ SWASCMTTSL QLAQECLRDG LPEPSEPPQP LEGLEMFAQT I ETVLRRIK VTFLDTVVRV EHSPGDGERG VAVEVRVQRL EYCDEAVRDP SQAPPVDVHQ PPAFLHKLLQ LAGVRLHYEE LP AQEEPPE PPLQIGSCSG YMELMVKLKQ NEAFPGPKLE VAGQLGSLHL LLTPRQLQQL QELLSAVSLT DHEGLADKLN KSR PLGAED LWLIEQDLNQ QLQAGAVAEP LSPDPLTNPL LNLDNTDLFF SMAGLTSSVA SALSELSLSD VDLASSVRSD MASR RLSAQ AHPAGKMAPN PLLDTMRPDS LLKMTLGGVT LTLLQTSAPS SGPPDLATHF FTEFDATKDG PFGSRDFHHL RPRFQ RACP CSHVRLTGTA VQLSWELRTG SRGRRTTSME VHFGQLEVLE CLWPRGTSEP EYTEILTFPG TLGSQASARP CAHLRH TQI LRRVPKSRPR RSVACHCHSE LALDLANFQA DVELGALDRL AALLRLATVP AEPPAGLLTE PLPAMEQQTV FRLSAPR AT LRLRFPIADL RPEPDPWAGQ AVRAEQLRLE LSEPQFRSEL SSGPGPPVPT HLELTCSDLH GIYEDGGKPP VPCLRVSK A LDPKSTGRKY FLPQVVVTVN PQSSSTQWEV APEKGEELEL SVESPCELRE PEPSPFSSKR TMYETEEMVI PGDPEEMRT FQSRTLALSR CSLEVILPSV HIFLPSKEVY ESIYNRINND LLMWEPADLL PTPDPAAQPS GFPGPSGFWH DSFKMCKSAF KLANCFDLT PDSDSDDEDA HFFSVGASGG PQAAAPEAPS LHLQSTFSTL VTVLKGRITA LCETKDEGGK RLEAVHGELV L DMEHGTLF SVSQYCGQPG LGYFCLEAEK ATLYHRAAVD DYPLPSHLDL PSFAPPAQLA PTIYPSEEGV TERGASGRKG QG RGPHMLS TAVRIHLDPH KNVKEFLVTL RLHKATLRHY MALPEQSWHS QLLEFLDVLD DPVLGYLPPT VITILHTHLF SCS VDYRPL YLPVRVLITA ETFTLSSNII MDTSTFLLRF ILDDSALYLS DKCEVETLDL RRDYVCVLDV DLLELVIKTW KGST EGKLS QPLFELRCSN NVVHVHSCAD SCALLVNLLQ YVMSTGDLHP PPRPPSPTEI AGQKLSESPA SLPSCPPVET ALINQ RDLA DALLDTERSL RELAQPSGGH LPQASPISVY LFPGERSGAP PPSPPVGGPA GSLGSCSEEK EDEREEEGDG DTLDSD EFC ILDAPGLGIP PRDGEPVVTQ LHPGPIVVRD GYFSRPIGST DLLRAPAHFP VPSTRVVLRE VSLVWHLYGG RDFGPHP GH RARTGLSGPR SSPSRCSGPN RPQNSWRTQG GSGRQHHVLM EIQLSKVSFQ HEVYPAEPAT GPAAPSQELE ERPLSRQV F IVQELEVRDR LASSQINKFL YLHTSERMPR RAHSNMLTIK ALHVAPTTNL GGPECCLRVS LMPLRLNVDQ DALFFLKDF FTSLVAGINP VVPGETSAEA RPETRAQPSS PLEGQAEGVE TTGSQEAPGG GHSPSPPDQQ PIYFREFRFT SEVPIWLDYH GKHVTMDQV GTFAGLLIGL AQLNCSELKL KRLCCRHGLL GVDKVLGYAL NEWLQDIRKN QLPGLLGGVG PMHSVVQLFQ G FRDLLWLP IEQYRKDGRL MRGLQRGAAS FGSSTASAAL ELSNRLVQAI QATAETVYDI LSPAAPVSRS LQDKRSARRL RR GQQPADL REGVAKAYDT VREGILDTAQ TICDVASRGH EQKGLTGAVG GVIRQLPPTV VKPLILATEA TSSLLGGMRN QIV PDAHKD HALKWRSDSA QD UniProtKB: Autophagy-related protein 2 homolog A |
-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: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 61.65 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |