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- EMDB-7563: Structure of the HIV-Nef tetherin cargo bound AP-1:Arf1 stable cl... -

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Basic information

Entry
Database: EMDB / ID: EMD-7563
TitleStructure of the HIV-Nef tetherin cargo bound AP-1:Arf1 stable closed trimer
Map dataHIV-Nef tetherin cargo bound AP-1:Arf1 stable closed trimer
Sample
  • Complex: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer
    • Protein or peptide: Bone marrow stromal antigen 2, Protein Nef chimera
    • Protein or peptide: AP-1 complex subunit beta-1
    • Protein or peptide: ADP-ribosylation factor 1
    • Protein or peptide: AP-1 complex subunit gamma-1
    • Protein or peptide: AP-1 complex subunit mu-1
    • Protein or peptide: AP-1 complex subunit sigma-3
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
KeywordsAP / HIV / Nef / trafficking / VIRAL PROTEIN / PROTEIN TRANSPORT
Function / homology
Function and homology information


negative regulation of plasmacytoid dendritic cell cytokine production / negative regulation of intracellular transport of viral material / response to interferon-beta / basolateral protein secretion / : / AP-1 adaptor complex / endosome to melanosome transport / Lysosome Vesicle Biogenesis / mitotic cleavage furrow ingression / trans-Golgi Network Vesicle Budding ...negative regulation of plasmacytoid dendritic cell cytokine production / negative regulation of intracellular transport of viral material / response to interferon-beta / basolateral protein secretion / : / AP-1 adaptor complex / endosome to melanosome transport / Lysosome Vesicle Biogenesis / mitotic cleavage furrow ingression / trans-Golgi Network Vesicle Budding / protein trimerization / response to interferon-alpha / platelet dense granule organization / Glycosphingolipid transport / metalloendopeptidase inhibitor activity / regulation of receptor internalization / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / melanosome assembly / Intra-Golgi traffic / regulation of Arp2/3 complex-mediated actin nucleation / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / Golgi Associated Vesicle Biogenesis / symbiont-mediated suppression of host apoptosis / Synthesis of PIPs at the Golgi membrane / symbiont-mediated suppression of host autophagy / clathrin adaptor activity / positive regulation of leukocyte proliferation / MHC class II antigen presentation / CD4 receptor binding / thioesterase binding / Nef Mediated CD4 Down-regulation / dendritic spine organization / determination of left/right symmetry / long-term synaptic depression / clathrin-coated vesicle / azurophil granule membrane / COPI-dependent Golgi-to-ER retrograde traffic / clathrin binding / Lysosome Vesicle Biogenesis / negative regulation of viral genome replication / Golgi Associated Vesicle Biogenesis / cell leading edge / MHC class I protein binding / Synthesis of PIPs at the plasma membrane / B cell activation / host cell Golgi membrane / response to type II interferon / intracellular copper ion homeostasis / protein targeting / COPI-mediated anterograde transport / side of membrane / vesicle-mediated transport / clathrin-coated pit / regulation of calcium-mediated signaling / viral life cycle / Neutrophil degranulation / multivesicular body / MHC class II antigen presentation / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cytoplasmic vesicle membrane / negative regulation of cell migration / Nef mediated downregulation of MHC class I complex cell surface expression / sarcomere / small monomeric GTPase / trans-Golgi network membrane / kidney development / regulation of actin cytoskeleton organization / intracellular protein transport / trans-Golgi network / negative regulation of cell growth / response to virus / cellular response to virus / SH3 domain binding / virion component / SARS-CoV-1 activates/modulates innate immune responses / Interferon alpha/beta signaling / synaptic vesicle / presynapse / heart development / ATPase binding / defense response to virus / positive regulation of canonical NF-kappaB signal transduction / early endosome / neuron projection / postsynaptic density / symbiont-mediated suppression of host innate immune response / apical plasma membrane / protein domain specific binding / membrane raft / Golgi membrane / signaling receptor binding / lysosomal membrane / innate immune response / focal adhesion / GTPase activity / intracellular membrane-bounded organelle / synapse / Neutrophil degranulation / protein kinase binding / GTP binding
Similarity search - Function
Bone marrow stromal antigen 2 / Bone marrow stromal antigen 2 / AP-1 complex subunit sigma / Adaptor protein complex AP-1, gamma subunit / Gamma-adaptin ear (GAE) domain / Gamma-adaptin ear (GAE) domain profile. / HIV-1 Nef protein, anchor domain superfamily / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / HIV negative factor Nef ...Bone marrow stromal antigen 2 / Bone marrow stromal antigen 2 / AP-1 complex subunit sigma / Adaptor protein complex AP-1, gamma subunit / Gamma-adaptin ear (GAE) domain / Gamma-adaptin ear (GAE) domain profile. / HIV-1 Nef protein, anchor domain superfamily / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / HIV negative factor Nef / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit / HIV-1 Nef protein, core domain superfamily / Negative factor, (F-Protein) or Nef / : / Beta-adaptin appendage, C-terminal subdomain / Beta2-adaptin appendage, C-terminal sub-domain / ADP-ribosylation factor 1-5 / AP complex subunit beta / Clathrin adaptor complex, small chain / Clathrin adaptor complexes small chain signature. / Clathrin adaptor complexes medium chain signature 1. / Clathrin adaptor, mu subunit / Clathrin adaptor, mu subunit, conserved site / Clathrin adaptor complexes medium chain signature 2. / : / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Adaptin C-terminal domain / Adaptin C-terminal domain / AP complex, mu/sigma subunit / Clathrin adaptor complex small chain / Adaptor complexes medium subunit family / AP-2 complex subunit mu, C-terminal superfamily / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / Mu homology domain / Mu homology domain (MHD) profile. / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Small GTPase superfamily, ARF type / small GTPase Arf family profile. / Sar1p-like members of the Ras-family of small GTPases / Small GTPase superfamily, ARF/SAR type / ADP-ribosylation factor family / Longin-like domain superfamily / ARF-like small GTPases; ARF, ADP-ribosylation factor / TBP domain superfamily / Armadillo/beta-catenin-like repeats / Armadillo / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
AP-1 complex subunit gamma-1 / AP-1 complex subunit mu-1 / ADP-ribosylation factor 1 / AP-1 complex subunit beta-1 / Bone marrow stromal antigen 2 / Protein Nef / AP-1 complex subunit sigma-3
Similarity search - Component
Biological speciesHomo sapiens (human) / Human immunodeficiency virus 1 / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.8 Å
AuthorsMorris KL / Buffalo CZ / Hurley JH
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI 120691 United States
CitationJournal: Cell / Year: 2018
Title: HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation.
Authors: Kyle L Morris / Cosmo Z Buffalo / Christina M Stürzel / Elena Heusinger / Frank Kirchhoff / Xuefeng Ren / James H Hurley /
Abstract: The HIV accessory protein Nef counteracts immune defenses by subverting coated vesicle pathways. The 3.7 Å cryo-EM structure of a closed trimer of the clathrin adaptor AP-1, the small GTPase Arf1, ...The HIV accessory protein Nef counteracts immune defenses by subverting coated vesicle pathways. The 3.7 Å cryo-EM structure of a closed trimer of the clathrin adaptor AP-1, the small GTPase Arf1, HIV-1 Nef, and the cytosolic tail of the restriction factor tetherin suggested a mechanism for inactivating tetherin by Golgi retention. The 4.3 Å structure of a mutant Nef-induced dimer of AP-1 showed how the closed trimer is regulated by the dileucine loop of Nef. HDX-MS and mutational analysis were used to show how cargo dynamics leads to alternative Arf1 trimerization, directing Nef targets to be either retained at the trans-Golgi or sorted to lysosomes. Phosphorylation of the NL4-3 M-Nef was shown to regulate AP-1 trimerization, explaining how O-Nefs lacking this phosphosite counteract tetherin but most M-Nefs do not. These observations show how the higher-order organization of a vesicular coat can be allosterically modulated to direct cargoes to distinct fates.
History
DepositionMar 18, 2018-
Header (metadata) releaseApr 11, 2018-
Map releaseAug 1, 2018-
UpdateMay 14, 2025-
Current statusMay 14, 2025Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0149
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.0149
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6cri
  • Surface level: 0.0149
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_7563.png

Downloads & links

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Map

FileDownload / File: emd_7563.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationHIV-Nef tetherin cargo bound AP-1:Arf1 stable closed trimer
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 384 pix.
= 409.728 Å		1.07 Å/pix.
x 384 pix.
= 409.728 Å		1.07 Å/pix.
x 384 pix.
= 409.728 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.067 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0149 / Movie #1: 0.0149
Minimum - Maximum-0.017942984 - 0.058546383
Average (Standard dev.)0.0003145799 (±0.002489533)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 409.72803 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0671.0671.067
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z409.728409.728409.728
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-0.0180.0590.000

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Supplemental data

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Sample components

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Entire : Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed...

EntireName: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer
Components
  • Complex: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer
    • Protein or peptide: Bone marrow stromal antigen 2, Protein Nef chimera
    • Protein or peptide: AP-1 complex subunit beta-1
    • Protein or peptide: ADP-ribosylation factor 1
    • Protein or peptide: AP-1 complex subunit gamma-1
    • Protein or peptide: AP-1 complex subunit mu-1
    • Protein or peptide: AP-1 complex subunit sigma-3
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed...

SupramoleculeName: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 700 KDa

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Macromolecule #1: Bone marrow stromal antigen 2, Protein Nef chimera

MacromoleculeName: Bone marrow stromal antigen 2, Protein Nef chimera / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Human immunodeficiency virus 1
Molecular weightTheoretical: 29.964326 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSYYHHHHHH DYDIPTTENL YFQGAMGSAS TSYDYCRVPM EDGDKRCKGS DEASEGSGMG GKWSKSSVIG WPAVRERMRR AEPAADGVG AVSRDLEKHG AITSSNTAAN NAACAWLEAQ EEEEVGFPVT PQVPLRPMTY KAAVDLSHFL KEKGGLEGLI H SQRRQDIL ...String:
MSYYHHHHHH DYDIPTTENL YFQGAMGSAS TSYDYCRVPM EDGDKRCKGS DEASEGSGMG GKWSKSSVIG WPAVRERMRR AEPAADGVG AVSRDLEKHG AITSSNTAAN NAACAWLEAQ EEEEVGFPVT PQVPLRPMTY KAAVDLSHFL KEKGGLEGLI H SQRRQDIL DLWIYHTQGY FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP DKVEEANKGE NTSLLHPVSL HGMDDPEREV LE WRFDSRL AFHHVARELH PEYFKNC

UniProtKB: Bone marrow stromal antigen 2, Protein Nef

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Macromolecule #2: AP-1 complex subunit beta-1

MacromoleculeName: AP-1 complex subunit beta-1 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 64.458656 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: EIFELKAELN SDKKEKKKEA VKKVIASMTV GKDVSALFPD VVNCMQTDNL ELKKLVYLYL MNYAKSQPDM AIMAVNTFVK DCEDPNPLI RALAVRTMGC IRVDKITEYL CEPLRKCLKD EDPYVRKTAA VCVAKLHDIN AQLVEDQGFL DTLKDLISDS N PMVVANAV ...String:
EIFELKAELN SDKKEKKKEA VKKVIASMTV GKDVSALFPD VVNCMQTDNL ELKKLVYLYL MNYAKSQPDM AIMAVNTFVK DCEDPNPLI RALAVRTMGC IRVDKITEYL CEPLRKCLKD EDPYVRKTAA VCVAKLHDIN AQLVEDQGFL DTLKDLISDS N PMVVANAV AALSEIAESH PSSNLLDLNP QSINKLLTAL NECTEWGQIF ILDCLANYMP KDDREAQSIC ERVTPRLSHA NS AVVLSAV KVLMKFMEML SKDLDYYGTL LKKLAPPLVT LLSAEPELQY VALRNINLIV QKRPEILKHE MKVFFVKYND PIY VKLEKL DIMIRLASQA NIAQVLAELR EYATEVDVDF VRKAVRAIGR CAIKVEQSAE RCVSTLLDLI QTKVNYVVQE AIVV IKDIF RKYPNKYESV IATLCENLDS LDEPEARAAM IWIVGEYAER IDNADELLES FLEGFHDKST QVQLQLLTAI VKLFL KKPT ETQELVQQVL SLATQDSDNP DLRDRGYIYW RLLSTDPVAA KEVVLAEKPL ISEETDLIEP TLLDELICYI GTLASV YHK PPSAFVE

UniProtKB: AP-1 complex subunit beta-1

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Macromolecule #3: ADP-ribosylation factor 1

MacromoleculeName: ADP-ribosylation factor 1 / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.9366 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
EMRILMVGLD AAGKTTILYK LKLGEIVTTI PTIGFNVETV EYKNISFTVW DVGGLDKIRP LWRHYFQNTQ GLIFVVDSND RERVNEARE ELMRMLAEDE LRDAVLLVFA NKQDLPNAMN AAEITDKLGL HSLRHRNWYI QATCATSGDG LYEGLDWLSN Q LRNQK

UniProtKB: ADP-ribosylation factor 1

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Macromolecule #4: AP-1 complex subunit gamma-1

MacromoleculeName: AP-1 complex subunit gamma-1 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 66.401055 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: PIRLRELIRT IRTARTQAEE REMIQKECAA IRSSFREEDN TYRCRNVAKL LYMHMLGYPA HFGQLECLKL IASQKFTDKR IGYLGAMLL LDERQDVHLL MTNCIKNDLN HSTQFVQGLA LCTLGCMGSS EMCRDLAGEV EKLLKTSNSY LRKKAALCAV H VIRKVPEL ...String:
PIRLRELIRT IRTARTQAEE REMIQKECAA IRSSFREEDN TYRCRNVAKL LYMHMLGYPA HFGQLECLKL IASQKFTDKR IGYLGAMLL LDERQDVHLL MTNCIKNDLN HSTQFVQGLA LCTLGCMGSS EMCRDLAGEV EKLLKTSNSY LRKKAALCAV H VIRKVPEL MEMFLPATKN LLNEKNHGVL HTSVVLLTEM CERSPDMLAH FRKLVPQLVR ILKNLIMSGY SPEHDVSGIS DP FLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK SESGLRVLAI NILGRFLLNN DKN IRYVAL TSLLKTVQTD HNAVQRHRST IVDCLKDLDV SIKRRAMELS FALVNGNNIR GMMKELLYFL DSCEPEFKAD CASG IFLAA EKYAPSKRWH IDTIMRVLTT AGSYVRDDAV PNLIQLITNS VEMHAYTVQR LYKAILGDYS QQPLVQVAAW CIGEY GDLL VSGQCEEEEP IQVTEDEVLD ILESVLISNM STSVTRGYAL TAIMKLSTRF TCTVNRIKKV VSIYGSSIDV ELQQRA VEY NALFKKYDHM RSALLERMPV ME

UniProtKB: AP-1 complex subunit gamma-1

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Macromolecule #5: AP-1 complex subunit mu-1

MacromoleculeName: AP-1 complex subunit mu-1 / type: protein_or_peptide / ID: 5 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 48.475535 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: SASAVYVLDL KGKVLICRNY RGDVDMSEVE HFMPILMEKE EEGMLSPILA HGGVRFMWIK HNNLYLVATS KKNACVSLVF SFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR S EGIKYRKN ...String:
SASAVYVLDL KGKVLICRNY RGDVDMSEVE HFMPILMEKE EEGMLSPILA HGGVRFMWIK HNNLYLVATS KKNACVSLVF SFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR S EGIKYRKN EVFLDVIEAV NLLVSANGNV LRSEIVGSIK MRVFLSGMPE LRLGLNDKVL FDNTGRGKSK SVELEDVKFH QC VRLSRFE NDRTISFIPP DGEFELMSYR LNTHVKPLIW IESVIEKHSH SRIEYMVKAK SQFKRRSTAN NVEIHIPVPN DAD SPKFKT TVGSVKWVPE NSEIVWSVKS FPGGKEYLMR AHFGLPSVEA EDKEGKPPIS VKFEIPYFTT SGIQVRYLKI IEKS GYQAL PWVRYITQNG DYQLRTQ

UniProtKB: AP-1 complex subunit mu-1

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Macromolecule #6: AP-1 complex subunit sigma-3

MacromoleculeName: AP-1 complex subunit sigma-3 / type: protein_or_peptide / ID: 6 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.99885 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MIHFILLFSR QGKLRLQKWY ITLPDKERKK ITREIVQIIL SRGHRTSSFV DWKELKLVYK RYASLYFCCA IENQDNELLT LEIVHRYVE LLDKYFGNVC ELDIIFNFEK AYFILDEFII GGEIQETSKK IAVKAIEDSD MLQ

UniProtKB: AP-1 complex subunit sigma-3

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Macromolecule #7: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 6 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

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Macromolecule #8: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 8 / Number of copies: 6 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.07 mg/mL
BufferpH: 8
Details: 20 mM Tris at pH 8.0, 200 mM NaCl, 5 mM MgCl2, and 0.5 mM TCEP
GridPretreatment - Type: PLASMA CLEANING / Details: unspecified
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 296 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 62.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: CRYOSPARC
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 6.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 11108
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Overall B value: 425 / Target criteria: Correlation coefficient
Output model

PDB-6cri:
Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer

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