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- EMDB-12220: VPS35/VPS29 arch of metazoan membrane-assembled retromer:SNX3 complex -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-12220 | ||||||||||||||||||
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Title | VPS35/VPS29 arch of metazoan membrane-assembled retromer:SNX3 complex | ||||||||||||||||||
![]() | LAFTER-filtered map of VP35 arch of metazoan retromer:SNX3 complex | ||||||||||||||||||
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![]() | endosomes / coat proteins / membrane trafficking / cargo-sorting / ENDOCYTOSIS | ||||||||||||||||||
Function / homology | ![]() neurotransmitter receptor transport, endosome to plasma membrane / negative regulation of protein localization / regulation of dendritic spine maintenance / mitochondrion-derived vesicle / negative regulation of protein homooligomerization / tubular endosome / positive regulation of Wnt protein secretion / regulation of terminal button organization / mitochondrion to lysosome vesicle-mediated transport / WNT ligand biogenesis and trafficking ...neurotransmitter receptor transport, endosome to plasma membrane / negative regulation of protein localization / regulation of dendritic spine maintenance / mitochondrion-derived vesicle / negative regulation of protein homooligomerization / tubular endosome / positive regulation of Wnt protein secretion / regulation of terminal button organization / mitochondrion to lysosome vesicle-mediated transport / WNT ligand biogenesis and trafficking / retromer, cargo-selective complex / positive regulation of locomotion involved in locomotory behavior / negative regulation of lysosomal protein catabolic process / negative regulation of late endosome to lysosome transport / positive regulation of dopamine receptor signaling pathway / mitochondrial fragmentation involved in apoptotic process / vesicle-mediated transport in synapse / positive regulation of dopamine biosynthetic process / neurotransmitter receptor transport, endosome to postsynaptic membrane / protein localization to endosome / retromer complex / voluntary musculoskeletal movement / regulation of protein metabolic process / dopaminergic synapse / regulation of synapse maturation / transcytosis / endocytic recycling / retrograde transport, endosome to Golgi / regulation of mitochondrion organization / positive regulation of protein localization to cell periphery / lysosome organization / positive regulation of mitochondrial fission / regulation of postsynapse assembly / regulation of presynapse assembly / D1 dopamine receptor binding / regulation of macroautophagy / intracellular protein transport / modulation of chemical synaptic transmission / regulation of protein stability / protein destabilization / Wnt signaling pathway / negative regulation of inflammatory response / positive regulation of protein catabolic process / positive regulation of canonical Wnt signaling pathway / late endosome / presynapse / early endosome / lysosome / endosome / postsynaptic density / endosome membrane / neuron projection / lysosomal membrane / negative regulation of gene expression / intracellular membrane-bounded organelle / neuronal cell body / positive regulation of gene expression / perinuclear region of cytoplasm / glutamatergic synapse / extracellular exosome / metal ion binding / cytosol Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | subtomogram averaging / cryo EM / Resolution: 8.9 Å | ||||||||||||||||||
![]() | Leneva N / Kovtun O | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly. Authors: Natalya Leneva / Oleksiy Kovtun / Dustin R Morado / John A G Briggs / David J Owen / ![]() Abstract: Retromer is a master regulator of cargo retrieval from endosomes, which is critical for many cellular processes including signaling, immunity, neuroprotection, and virus infection. The retromer core ...Retromer is a master regulator of cargo retrieval from endosomes, which is critical for many cellular processes including signaling, immunity, neuroprotection, and virus infection. The retromer core (VPS26/VPS29/VPS35) is present on cargo-transporting, tubular carriers along with a range of sorting nexins. Here, we elucidate the structural basis of membrane tubulation and coupled cargo recognition by metazoan and fungal retromer coats assembled with the non-Bin1/Amphiphysin/Rvs (BAR) sorting nexin SNX3 using cryo-electron tomography. The retromer core retains its arched, scaffolding structure but changes its mode of membrane recruitment when assembled with different SNX adaptors, allowing cargo recognition at subunit interfaces. Thus, membrane bending and cargo incorporation can be modulated to allow retromer to traffic cargoes along different cellular transport routes. | ||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.9 KB 17.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 6.1 KB | Display | ![]() |
Images | ![]() | 107.4 KB | ||
Masks | ![]() | 18.1 MB | ![]() | |
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 16.7 MB 16.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 749.9 KB | Display | ![]() |
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Full document | ![]() | 749.5 KB | Display | |
Data in XML | ![]() | 11.5 KB | Display | |
Data in CIF | ![]() | 15.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7blnMC ![]() 7bloC ![]() 7blpC ![]() 7blqC ![]() 7blrC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | |
EM raw data | ![]() Data size: 764.9 Data #1: Raw image frames for the metazoan retromer:SNX3 coat assembled on the Wls cargo-containing membranes [micrographs - multiframe] Data #2: Corrected, aligned and order-sorted tilt series for the metazoan retromer:SNX3 coat assembled on the Wls cargo-containing membranes [tilt series] Data #3: Corrected, aligned, dose-filtered and order-sorted tilt series for the metazoan retromer:SNX3 coat assembled on the Wls cargo-containing membranes [tilt series]) |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | LAFTER-filtered map of VP35 arch of metazoan retromer:SNX3 complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.701 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: half-map1 of VP35 arch of metazoan retromer:SNX3 complex
File | emd_12220_half_map_1.map | ||||||||||||
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Annotation | half-map1 of VP35 arch of metazoan retromer:SNX3 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half-map2 of VP35 arch of metazoan retromer:SNX3 complex
File | emd_12220_half_map_2.map | ||||||||||||
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Annotation | half-map2 of VP35 arch of metazoan retromer:SNX3 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : arch assembly (VPS35/VPS29) of the metazoan retromer:SNX3 complex.
Entire | Name: arch assembly (VPS35/VPS29) of the metazoan retromer:SNX3 complex. |
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Components |
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-Supramolecule #1: arch assembly (VPS35/VPS29) of the metazoan retromer:SNX3 complex.
Supramolecule | Name: arch assembly (VPS35/VPS29) of the metazoan retromer:SNX3 complex. type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: metazoan retromer:SNX3 complex assembled on liposomes containing Wls cargo peptide. |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Vacuolar protein sorting-associated protein 29
Macromolecule | Name: Vacuolar protein sorting-associated protein 29 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 20.531705 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR GDFDENLNYP EQKVVTVGQF KIGLIHGHQ VIPWGDMASL ALLQRQFDVD ILISGHTHKF EAFEHENKFY INPGSATGAY NALETNIIPS FVLMDIQAST V VTYVYQLI GDDVKVERIE YKKP UniProtKB: Vacuolar protein sorting-associated protein 29 |
-Macromolecule #2: Vacuolar protein sorting-associated protein 35
Macromolecule | Name: Vacuolar protein sorting-associated protein 35 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 91.816805 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP KSYYELYMAI SDELHYLEVY LTDEFAKGR KVADLYELVQ YAGNIIPRLY LLITVGVVYV KSFPQSRKDI LKDLVEMCRG VQHPLRGLFL RNYLLQCTRN I LPDEGEPT ...String: MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP KSYYELYMAI SDELHYLEVY LTDEFAKGR KVADLYELVQ YAGNIIPRLY LLITVGVVYV KSFPQSRKDI LKDLVEMCRG VQHPLRGLFL RNYLLQCTRN I LPDEGEPT DEETTGDISD SMDFVLLNFA EMNKLWVRMQ HQGHSRDREK RERERQELRI LVGTNLVRLS QLEGVNVERY KQ IVLTGIL EQVVNCRDAL AQEYLMECII QVFPDEFHLQ TLNPFLRACA ELHQNVNVKN IIIALIDRLA LFAHREDGPG IPA DIKLFD IFSQQVATVI QSRQDMPSED VVSLQVSLIN LAMKCYPDRV DYVDKVLETT VEIFNKLNLE HIATSSAVSK ELTR LLKIP VDTYNNILTV LKLKHFHPLF EYFDYESRKS MSCYVLSNVL DYNTEIVSQD QVDSIMNLVS TLIQDQPDQP VEDPD PEDF ADEQSLVGRF IHLLRSEDPD QQYLILNTAR KHFGAGGNQR IRFTLPPLVF AAYQLAFRYK ENSKVDDKWE KKCQKI FSF AHQTISALIK AELAELPLRL FLQGALAAGE IGFENHETVA YEFMSQAFSL YEDEISDSKA QLAAITLIIG TFERMKC FS EENHEPLRTQ CALAASKLLK KPDQGRAVST CAHLFWSGRN TDKNGEELHG GKRVMECLKK ALKIANQCMD PSLQVQLF I EILNRYIYFY EKENDAVTIQ VLNQLIQKIR EDLPNLESSE ETEQINKHFH NTLEHLRLRR ESPESEGPIY EGLIL UniProtKB: Vacuolar protein sorting-associated protein 35 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | subtomogram averaging |
Aggregation state | 3D array |
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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 BIOQUANTUM (6k x 4k) / Average electron dose: 3.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT | ||||||||
Output model | ![]() PDB-7bln: |