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- EMDB-12224: Vps26 dimer region of the fungal membrane-assembled retromer:Grd1... -

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Basic information

Entry
Database: EMDB / ID: EMD-12224
TitleVps26 dimer region of the fungal membrane-assembled retromer:Grd19 complex.
Map dataSharpened, locally filtered map of VPS26 dimer region of the fungal retromer:Grd19 complex assembled on the membrane
Sample
  • Complex: Vps26 dimer region of the fungal membrane-assembled retromer:Grd19 cargo-containing complex
    • Protein or peptide: Vacuolar protein sorting-associated protein 35Vacuole
    • Protein or peptide: Sorting nexin-3
    • Protein or peptide: Vacuolar protein sorting-associated protein 26-like proteinVacuole
    • Protein or peptide: The C-terminal portion of Kex2 cargo, fitted with Phi-X-(L/M) sorting motif of hDMT1-II cargo.
  • Ligand: 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE
Function / homology
Function and homology information


vanadium ion transmembrane transporter activity / vanadium ion transport / transition metal ion transmembrane transporter activity / paraferritin complex / Defective SLC11A2 causes hypochromic microcytic anemia, with iron overload 1 (AHMIO1) / lead ion transmembrane transporter activity / nickel cation transmembrane transporter activity / lead ion transport / cadmium ion transmembrane transport / nickel cation transport ...vanadium ion transmembrane transporter activity / vanadium ion transport / transition metal ion transmembrane transporter activity / paraferritin complex / Defective SLC11A2 causes hypochromic microcytic anemia, with iron overload 1 (AHMIO1) / lead ion transmembrane transporter activity / nickel cation transmembrane transporter activity / lead ion transport / cadmium ion transmembrane transport / nickel cation transport / solute:proton symporter activity / inorganic cation transmembrane transporter activity / Metal ion SLC transporters / manganese ion transport / iron ion transmembrane transport / manganese ion transmembrane transporter activity / zinc ion transmembrane transporter activity / detection of oxygen / iron ion transmembrane transporter activity / cadmium ion transmembrane transporter activity / cobalt ion transport / retromer, cargo-selective complex / cobalt ion transmembrane transporter activity / iron import into cell / retromer complex binding / copper ion transmembrane transporter activity / ferrous iron transmembrane transporter activity / copper ion transport / basal part of cell / phosphatidylinositol-3-phosphate binding / vacuole / retrograde transport, endosome to Golgi / response to iron ion / dendrite morphogenesis / heme biosynthetic process / erythrocyte development / cadmium ion binding / brush border membrane / Iron uptake and transport / intracellular protein transport / trans-Golgi network / recycling endosome / multicellular organismal-level iron ion homeostasis / recycling endosome membrane / activation of cysteine-type endopeptidase activity involved in apoptotic process / extracellular vesicle / protein transport / late endosome / apical part of cell / late endosome membrane / cellular response to oxidative stress / iron ion transport / cytoplasmic vesicle / early endosome membrane / intracellular iron ion homeostasis / mitochondrial outer membrane / lysosome / response to hypoxia / learning or memory / early endosome / apical plasma membrane / lysosomal membrane / Golgi membrane / perinuclear region of cytoplasm / Golgi apparatus / cell surface / mitochondrion / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Fungal SNX3, PX domain / Vacuolar protein sorting protein 26 related / Vacuolar protein sorting-associated protein 26 / Vacuolar protein sorting-associated protein 35 / Vacuolar protein sorting-associated protein 35, C-terminal / Vacuolar protein sorting-associated protein 35 / NRAMP family / Natural resistance-associated macrophage protein-like / Arrestin-like, C-terminal / PhoX homologous domain, present in p47phox and p40phox. ...Fungal SNX3, PX domain / Vacuolar protein sorting protein 26 related / Vacuolar protein sorting-associated protein 26 / Vacuolar protein sorting-associated protein 35 / Vacuolar protein sorting-associated protein 35, C-terminal / Vacuolar protein sorting-associated protein 35 / NRAMP family / Natural resistance-associated macrophage protein-like / Arrestin-like, C-terminal / PhoX homologous domain, present in p47phox and p40phox. / PX domain profile. / PX domain / Phox homology / PX domain superfamily
Similarity search - Domain/homology
Vacuolar protein sorting-associated protein 26-like protein / Sorting nexin-3 / Vacuolar protein sorting-associated protein 35 / Natural resistance-associated macrophage protein 2
Similarity search - Component
Biological speciesChaetomium thermophilum var. thermophilum DSM 1495 (fungus) / Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Methodsubtomogram averaging / cryo EM / Resolution: 9.2 Å
AuthorsLeneva N / Kovtun O / Morado DR / Briggs JAG / Owen DJ
Funding support United Kingdom, 5 items
OrganizationGrant numberCountry
Wellcome Trust207455/Z/17/Z United Kingdom
Wellcome Trust206171/Z/17/Z United Kingdom
Wellcome Trust202905/Z/16/Z United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UP_1201/16 United Kingdom
European Research Council (ERC)ERC-CoG-648432 MEMBRANEFUSION United Kingdom
CitationJournal: Sci Adv / Year: 2021
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
DepositionJan 18, 2021-
Header (metadata) releaseMar 3, 2021-
Map releaseMar 3, 2021-
UpdateApr 7, 2021-
Current statusApr 7, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.235
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.235
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7blq
  • Surface level: 0.235
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12224.png

Downloads & links

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Map

FileDownload / File: emd_12224.map.gz / Format: CCP4 / Size: 3.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened, locally filtered map of VPS26 dimer region of the fungal retromer:Grd19 complex assembled on the membrane
Voxel sizeX=Y=Z: 2.758 Å
Density
Contour LevelBy AUTHOR: 0.235 / Movie #1: 0.235
Minimum - Maximum-0.5964883 - 1.1464814
Average (Standard dev.)0.0036801388 (±0.063661784)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions100100100
Spacing100100100
CellA=B=C: 275.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.7582.7582.758
M x/y/z100100100
origin x/y/z0.0000.0000.000
length x/y/z275.800275.800275.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS100100100
D min/max/mean-0.5961.1460.004

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Supplemental data

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Mask #1

Fileemd_12224_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half-map2

Fileemd_12224_half_map_1.map
Annotationhalf-map2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half-map1

Fileemd_12224_half_map_2.map
Annotationhalf-map1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Vps26 dimer region of the fungal membrane-assembled retromer:Grd1...

EntireName: Vps26 dimer region of the fungal membrane-assembled retromer:Grd19 cargo-containing complex
Components
  • Complex: Vps26 dimer region of the fungal membrane-assembled retromer:Grd19 cargo-containing complex
    • Protein or peptide: Vacuolar protein sorting-associated protein 35Vacuole
    • Protein or peptide: Sorting nexin-3
    • Protein or peptide: Vacuolar protein sorting-associated protein 26-like proteinVacuole
    • Protein or peptide: The C-terminal portion of Kex2 cargo, fitted with Phi-X-(L/M) sorting motif of hDMT1-II cargo.
  • Ligand: 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE

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Supramolecule #1: Vps26 dimer region of the fungal membrane-assembled retromer:Grd1...

SupramoleculeName: Vps26 dimer region of the fungal membrane-assembled retromer:Grd19 cargo-containing complex
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Details: fungal retromer:Grd19 complex assembled on liposomes containing Kex2 cargo peptide.
Source (natural)Organism: Chaetomium thermophilum var. thermophilum DSM 1495 (fungus)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #1: Vacuolar protein sorting-associated protein 35

MacromoleculeName: Vacuolar protein sorting-associated protein 35 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719
Molecular weightTheoretical: 34.014195 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: RLLEDALIAV RQQTAMMRKF LDTPGKLMDA LKCCSTLVSE LRTSSLSPKQ YYELYMAVFD ALRYLSAHLR ENHPVNHLAD LYELVQYAG NIIPRLYLMI TVGTAYMSID GAPVKELMKD MMDMSRGVQH PVRGLFLRYY LSGQARDYLP TGDSDGPEGN L QDSINFIL ...String:
RLLEDALIAV RQQTAMMRKF LDTPGKLMDA LKCCSTLVSE LRTSSLSPKQ YYELYMAVFD ALRYLSAHLR ENHPVNHLAD LYELVQYAG NIIPRLYLMI TVGTAYMSID GAPVKELMKD MMDMSRGVQH PVRGLFLRYY LSGQARDYLP TGDSDGPEGN L QDSINFIL TNFVEMNKLW VRLQHQGHSR ERDLRTQERR ELQLLVGSNI VRLSQLVDLP TYRDSILGPL LEQIVQCRDI LA QEYLLEV ITQVFPDEYH LHTLDQFLGA VSRLNPHVNV KAIVIGMMNR LSDYAERE

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Macromolecule #2: Sorting nexin-3

MacromoleculeName: Sorting nexin-3 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719
Molecular weightTheoretical: 13.52549 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
PPENFLEIEV RNPQTHGVGR HMYTDYEIVC RTNIPAFKLR QSSVRRRYSD FEYFRDILER ESARVTIPPL PGKVFTNRFS DEVIENRRA GLEKFLKIVV GHPLLQTGSK VLAAFVQ

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Macromolecule #3: Vacuolar protein sorting-associated protein 26-like protein

MacromoleculeName: Vacuolar protein sorting-associated protein 26-like protein
type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719
Molecular weightTheoretical: 34.308449 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: FSTPVDIDIV LADADKRAMV DVKLDKNRRE KVPLYMDGES VKGCVTVRPK DGKRLEHTGI KVQFIGTIEM FFDRGNHYEF LSLVQELAA PGELQHPQTF DFNFKNVEKQ YESYNGINVK LRYFVRVTVS RRMADVIREK DIWVYSYRIP PELNSSIKMD V GIEDCLHI ...String:
FSTPVDIDIV LADADKRAMV DVKLDKNRRE KVPLYMDGES VKGCVTVRPK DGKRLEHTGI KVQFIGTIEM FFDRGNHYEF LSLVQELAA PGELQHPQTF DFNFKNVEKQ YESYNGINVK LRYFVRVTVS RRMADVIREK DIWVYSYRIP PELNSSIKMD V GIEDCLHI EFEYSKSKYH LKDVIVGRIY FLLVRLKIKH MELSIIRRET TGVAPNQYNE SETLVRFEIM DGSPSRGETI PI RLFLGGF DLTPTFRDVN KKFSTRYYLS LVLIDEDARR YFKQSEIILY RQPPE

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Macromolecule #4: The C-terminal portion of Kex2 cargo, fitted with Phi-X-(L/M) sor...

MacromoleculeName: The C-terminal portion of Kex2 cargo, fitted with Phi-X-(L/M) sorting motif of hDMT1-II cargo.
type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chaetomium thermophilum var. thermophilum DSM 1495 (fungus)
Molecular weightTheoretical: 1.221422 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
QPELYLLNTM

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Macromolecule #5: 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOX...

MacromoleculeName: 2-(BUTANOYLOXY)-1-{[(HYDROXY{[2,3,4,6-TETRAHYDROXY-5-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL)OXY]METHYL}ETHYL BUTANOATE
type: ligand / ID: 5 / Number of copies: 2 / Formula: PIB
Molecular weightTheoretical: 554.374 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation state3D array

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 3.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

ExtractionNumber tomograms: 82 / Number images used: 449807
Final angle assignmentType: OTHER
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 9.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number subtomograms used: 49886
FSC plot (resolution estimation)

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