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- EMDB-40464: CCT G beta 5 complex intermediate state -

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Basic information

Entry
Database: EMDB / ID: EMD-40464
TitleCCT G beta 5 complex intermediate state
Map data
Sample
  • Complex: CCT-Gb5-PhLP1 in intermediate state
    • Protein or peptide: T-complex protein 1 subunit zeta
    • Protein or peptide: T-complex protein 1 subunit alpha
    • Protein or peptide: T-complex protein 1 subunit gamma
    • Protein or peptide: T-complex protein 1 subunit eta, N-terminally processed
    • Protein or peptide: T-complex protein 1 subunit theta
    • Protein or peptide: T-complex protein 1 subunit beta
    • Protein or peptide: T-complex protein 1 subunit delta
    • Protein or peptide: T-complex protein 1 subunit epsilon
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsCCT / Gb5 / complex / open / CHAPERONE
Function / homology
Function and homology information


zona pellucida receptor complex / scaRNA localization to Cajal body / positive regulation of protein localization to Cajal body / tubulin complex assembly / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body ...zona pellucida receptor complex / scaRNA localization to Cajal body / positive regulation of protein localization to Cajal body / tubulin complex assembly / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / Prefoldin mediated transfer of substrate to CCT/TriC / RHOBTB1 GTPase cycle / WD40-repeat domain binding / intermediate filament cytoskeleton / beta-tubulin binding / pericentriolar material / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein complex assembly / heterochromatin / RHOBTB2 GTPase cycle / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomerase activity / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / cilium / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / azurophil granule lumen / unfolded protein binding / melanosome / protein folding / cell body / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / protein stabilization / cytoskeleton / cadherin binding / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / cytosol / cytoplasm
Similarity search - Function
T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. ...T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family
Similarity search - Domain/homology
T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / T-complex protein 1 subunit beta / T-complex protein 1 subunit eta
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsWang S / Sass M / Willardson BM / Shen PS
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Eye Institute (NIH/NEI)R01 EY012287 United States
CitationJournal: Mol Cell / Year: 2023
Title: Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.
Authors: Shuxin Wang / Mikaila I Sass / Yujin Kwon / W Grant Ludlam / Theresa M Smith / Ethan J Carter / Nathan E Gladden / Margot Riggi / Janet H Iwasa / Barry M Willardson / Peter S Shen /
Abstract: The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, ...The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gβ, a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gβ from an unfolded molten globule to a fully folded β-propeller. These structures reveal the mechanism by which CCT directs Gβ folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual β sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state.
History
DepositionApr 12, 2023-
Header (metadata) releaseNov 1, 2023-
Map releaseNov 1, 2023-
UpdateNov 15, 2023-
Current statusNov 15, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40464.png

Downloads & links

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Map

FileDownload / File: emd_40464.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.058 Å
Density
Contour LevelBy AUTHOR: 0.0932
Minimum - Maximum-0.26721108 - 0.7655721
Average (Standard dev.)0.0045933416 (±0.030336391)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 317.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_40464_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_40464_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : CCT-Gb5-PhLP1 in intermediate state

EntireName: CCT-Gb5-PhLP1 in intermediate state
Components
  • Complex: CCT-Gb5-PhLP1 in intermediate state
    • Protein or peptide: T-complex protein 1 subunit zeta
    • Protein or peptide: T-complex protein 1 subunit alpha
    • Protein or peptide: T-complex protein 1 subunit gamma
    • Protein or peptide: T-complex protein 1 subunit eta, N-terminally processed
    • Protein or peptide: T-complex protein 1 subunit theta
    • Protein or peptide: T-complex protein 1 subunit beta
    • Protein or peptide: T-complex protein 1 subunit delta
    • Protein or peptide: T-complex protein 1 subunit epsilon
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: CCT-Gb5-PhLP1 in intermediate state

SupramoleculeName: CCT-Gb5-PhLP1 in intermediate state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney / Tissue: Kidney
Molecular weightTheoretical: 947.77 kDa/nm

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Macromolecule #1: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 55.789281 KDa
SequenceString: QAALAVNISA ARGLQDVLRT NLGPKGTMKM LVSGAGDIKL TKDGNVLLHE MQIQHPTASL IAKVATAQDD ITGDGTTSNV LIIGELLKQ ADLYISEGLH PRIITEGFEA AKEKALQFLE EVKVSREMDR ETLIDVARTS LRTKVHAELA DVLTEAVVDS I LAIKKQDE ...String:
QAALAVNISA ARGLQDVLRT NLGPKGTMKM LVSGAGDIKL TKDGNVLLHE MQIQHPTASL IAKVATAQDD ITGDGTTSNV LIIGELLKQ ADLYISEGLH PRIITEGFEA AKEKALQFLE EVKVSREMDR ETLIDVARTS LRTKVHAELA DVLTEAVVDS I LAIKKQDE PIDLFMIEIM EMKHKSETDT SLIRGLVLDH GARHPDMKKR VEDAYILTCN VSLEYEKTEV NSGFFYKSAE ER EKLVKAE RKFIEDRVKK IIELKRKVCG DSDKGFVVIN QKGIDPFSLD ALSKEGIVAL RRAKRRNMER LTLACGGVAL NSF DDLSPD CLGHAGLVYE YTLGEEKFTF IEKCNNPRSV TLLIKGPNKH TLTQIKDAVR DGLRAVKNAI DDGCVVPGAG AVEV AMAEA LIKHKPSVKG RAQLGVQAFA DALLIIPKVL AQNSGFDLQE TLVKIQAEHS ESGQLVGVDL NTGEPMVAAE VGVWD NYCV KKQLLHSCTV IATNILLVDE IMRA

UniProtKB: T-complex protein 1 subunit zeta

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Macromolecule #2: T-complex protein 1 subunit alpha

MacromoleculeName: T-complex protein 1 subunit alpha / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 58.243172 KDa
SequenceString: EGPLSVFGDR STGETIRSQN VMAAASIANI VKSSLGPVGL DKMLVDDIGD VTITNDGATI LKLLEVEHPA AKVLCELADL QDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI I GINGDFFA ...String:
EGPLSVFGDR STGETIRSQN VMAAASIANI VKSSLGPVGL DKMLVDDIGD VTITNDGATI LKLLEVEHPA AKVLCELADL QDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI I GINGDFFA NMVVDAVLAI KYTDIRGQPR YPVNSVNILK AHGRSQMESM LISGYALNCV VGSQGMPKRI VNAKIACLDF SL QKTKMKL GVQVVITDPE KLDQIRQRES DITKERIQKI LATGANVILT TGGIDDMCLK YFVEAGAMAV RRVLKRDLKR IAK ASGATI LSTLANLEGE ETFEAAMLGQ AEEVVQERIC DDELILIKNT KARTSASIIL RGANDFMCDE MERSLHDALC VVKR VLESK SVVPGGGAVE AALSIYLENY ATSMGSREQL AIAEFARSLL VIPNTLAVNA AQDSTDLVAK LRAFHNEAQV NPERK NLKW IGLDLSNGKP RDNKQAGVFE PTIVKVKSLK FATEAAITIL RIDDLIKLHP ES

UniProtKB: T-complex protein 1 subunit alpha

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Macromolecule #3: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney / Tissue: Kidney
Molecular weightTheoretical: 58.837996 KDa
SequenceString: GHRPVLVLSQ NTKRESGRKV QSGNINAAKT IADIIRTCLG PKSMMKMLLD PMGGIVMTND GNAILREIQV QHPAAKSMIE ISRTQDEEV GDGTTSVIIL AGEMLSVAEH FLEQQMHPTV VISAYRKALD DMISTLKKIS IPVDISDSDM MLNIINSSIT T KAISRWSS ...String:
GHRPVLVLSQ NTKRESGRKV QSGNINAAKT IADIIRTCLG PKSMMKMLLD PMGGIVMTND GNAILREIQV QHPAAKSMIE ISRTQDEEV GDGTTSVIIL AGEMLSVAEH FLEQQMHPTV VISAYRKALD DMISTLKKIS IPVDISDSDM MLNIINSSIT T KAISRWSS LACNIALDAV KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL LD SSLEYKK GESQTDIEIT REEDFTRILQ MEEEYIQQLC EDIIQLKPDV VITEKGISDL AQHYLMRANI TAIRRVRKTD NNR IARACG ARIVSRPEEL REDDVGTGAG LLEIKKIGDE YFTFITDCKD PKACTILLRG ASKEILSEVE RNLQDAMQVC RNVL LDPQL VPGGGASEMA VAHALTEKSK AMTGVEQWPY RAVAQALEVI PRTLIQNCGA STIRLLTSLR AKHTQENCET WGVNG ETGT LVDMKELGIW EPLAVKLQTY KTAVETAVLL LRIDDIVSGH KKKG

UniProtKB: T-complex protein 1 subunit gamma

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Macromolecule #4: T-complex protein 1 subunit eta, N-terminally processed

MacromoleculeName: T-complex protein 1 subunit eta, N-terminally processed
type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 56.369867 KDa
SequenceString: GTDSSQGIPQ LVSNISACQV IAEAVRTTLG PRGMDKLIVD GRGKATISND GATILKLLDV VHPAAKTLVD IAKSQDAEVG DGTTSVTLL AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ Q KAFFAKMV ...String:
GTDSSQGIPQ LVSNISACQV IAEAVRTTLG PRGMDKLIVD GRGKATISND GATILKLLDV VHPAAKTLVD IAKSQDAEVG DGTTSVTLL AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ Q KAFFAKMV VDAVMMLDDL LQLKMIGIKK VQGGALEDSQ LVAGVAFKKT FSYAGFEMQP KKYHNPKIAL LNVELELKAE KD NAEIRVH TVEDYQAIVD AEWNILYDKL EKIHHSGAKV VLSKLPIGDV ATQYFADRDM FCAGRVPEED LKRTMMACGG SIQ TSVNAL SADVLGRCQV FEETQIGGER YNFFTGCPKA KTCTFILRGG AEQFMEETER SLHDAIMIVR RAIKNDSVVA GGGA IEMEL SKYLRDYSRT IPGKQQLLIG AYAKALEIIP RQLCDNAGFD ATNILNKLRA RHAQGGTWYG VDINNEDIAD NFEAF VWEP AMVRINALTA ASEAACLIVS VDETIKNPRS

UniProtKB: T-complex protein 1 subunit eta

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Macromolecule #5: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 54.399461 KDa
SequenceString: VYRNIQACKE LAQTTRTAYG PNGMNKMVIN HLEKLFVTND AATILRELEV QHPAAKMIVM ASHMQEQEVG DGTNFVLVFA GALLELAEE LLRIGLSVSE VIEGYEIACR KAHEILPNLV CCSAKNLRDI DEVSSLLRTS IMSKQYGNEV FLAKLIAQAC V SIFPDSGH ...String:
VYRNIQACKE LAQTTRTAYG PNGMNKMVIN HLEKLFVTND AATILRELEV QHPAAKMIVM ASHMQEQEVG DGTNFVLVFA GALLELAEE LLRIGLSVSE VIEGYEIACR KAHEILPNLV CCSAKNLRDI DEVSSLLRTS IMSKQYGNEV FLAKLIAQAC V SIFPDSGH FNVDNIRVCK ILGSGISSSS VLHGMVFKKE TEGDVTSVKD AKIAVYSCPF DGMITETKGT VLIKTAEELM NF SKGEENL MDAQVKAIAD TGANVVVTGG KVADMALHYA NKYNIMLVRL NSKWDLRRLC KTVGATALPR LTPPVLEEMG HCD SVYLSE VGDTQVVVFK HEKEDGAIST IVLRGSTDNL MDDIERAVDD GVNTFKVLTR DKRLVPGGGA TEIELAKQIT SYGE TCPGL EQYAIKKFAE AFEAIPRALA ENSGVKANEV ISKLYAVHQE GNKNVGLDIE AEVPAVKDML EAGILDTYLG KYWAI KLAT NAAVTVLRVD QIIM

UniProtKB: T-complex protein 1 subunit theta

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Macromolecule #6: T-complex protein 1 subunit beta

MacromoleculeName: T-complex protein 1 subunit beta / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 56.490855 KDa
SequenceString: ASLSLAPVNI FKAGADEERA ETARLTSFIG AIAIGDLVKS TLGPKGMDKI LLSSGRDASL MVTNDGATIL KNIGVDNPAA KVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM N IAGTTLSS ...String:
ASLSLAPVNI FKAGADEERA ETARLTSFIG AIAIGDLVKS TLGPKGMDKI LLSSGRDASL MVTNDGATIL KNIGVDNPAA KVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM N IAGTTLSS KLLTHHKDHF TKLAVEAVLR LKGSGNLEAI HIIKKLGGSL ADSYLDEGFL LDKKIGVNQP KRIENAKILI AN TGMDTDK IKIFGSRVRV DSTAKVAEIE HAEKEKMKEK VERILKHGIN CFINRQLIYN YPEQLFGAAG VMAIEHADFA GVE RLALVT GGEIASTFDH PELVKLGSCK LIEEVMIGED KLIHFSGVAL GEACTIVLRG ATQQILDEAE RSLHDALCVL AQTV KDSRT VYGGGCSEML MAHAVTQLAN RTPGKEAVAM ESYAKALRML PTIIADNAGY DSADLVAQLR AAHSEGNTTA GLDMR EGTI GDMAILGITE SFQVKRQVLL SAAEAAEVIL RVDNIIKAAP RK

UniProtKB: T-complex protein 1 subunit beta

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Macromolecule #7: T-complex protein 1 subunit delta

MacromoleculeName: T-complex protein 1 subunit delta / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 56.242168 KDa
SequenceString: RGKGAYQDRD KPAQIRFSNI SAAKAVADAI RTSLGPKGMD KMIQDGKGDV TITNDGATIL KQMQVLHPAA RMLVELSKAQ DIEAGDGTT SVVIIAGSLL DSCTKLLQKG IHPTIISESF QKALEKGIEI LTDMSRPVEL SDRETLLNSA TTSLNSKVVS Q YSSLLSPM ...String:
RGKGAYQDRD KPAQIRFSNI SAAKAVADAI RTSLGPKGMD KMIQDGKGDV TITNDGATIL KQMQVLHPAA RMLVELSKAQ DIEAGDGTT SVVIIAGSLL DSCTKLLQKG IHPTIISESF QKALEKGIEI LTDMSRPVEL SDRETLLNSA TTSLNSKVVS Q YSSLLSPM SVNAVMKVID PATATSVDLR DIKIVKKLGG TIDDCELVEG LVLTQKVSNS GITRVEKAKI GLIQFCLSAP KT DMDNQIV VSDYAQMDRV LREERAYILN LVKQIKKTGC NVLLIQKSIL RDALSDLALH FLNKMKIMVI KDIEREDIEF ICK TIGTKP VAHIDQFTAD MLGSAELAEE VNLNGSGKLL KITGCASPGK TVTIVVRGSN KLVIEEAERS IHDALCVIRC LVKK RALIA GGGAPEIELA LRLTEYSRTL SGMESYCVRA FADAMEVIPS TLAENAGLNP ISTVTELRNR HAQGEKTAGI NVRKG GISN ILEELVVQPL LVSVSALTLA TETVRSILKI DDVVNT

UniProtKB: T-complex protein 1 subunit delta

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Macromolecule #8: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 59.618754 KDa
SequenceString: ASMGTLAFDE YGRPFLIIKD QDRKSRLMGL EALKSHIMAA KAVANTMRTS LGPNGLDKMM VDKDGDVTVT NDGATILSMM DVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK D TEPLIQTA ...String:
ASMGTLAFDE YGRPFLIIKD QDRKSRLMGL EALKSHIMAA KAVANTMRTS LGPNGLDKMM VDKDGDVTVT NDGATILSMM DVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK D TEPLIQTA KTTLGSKVVN SCHRQMAEIA VNAVLTVADM ERRDVDFELI KVEGKVGGRL EDTKLIKGVI VDKDFSHPQM PK KVEDAKI AILTCPFEPP KPKTKHKLDV TSVEDYKALQ KYEKEKFEEM IQQIKETGAN LAICQWGFDD EANHLLLQNN LPA VRWVGG PEIELIAIAT GGRIVPRFSE LTAEKLGFAG LVQEISFGTT KDKMLVIEQC KNSRAVTIFI RGGNKMIIEE AKRS LHDAL CVIRNLIRDN RVVYGGGAAE ISCALAVSQE ADKCPTLEQY AMRAFADALE VIPMALSENS GMNPIQTMTE VRARQ VKEM NPALGIDCLH KGTNDMKQQH VIETLIGKKQ QISLATQMVR MILKIDDIRK PGESEE

UniProtKB: T-complex protein 1 subunit epsilon

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 16 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

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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

Concentration1.5 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMNaClSodium chloridesodium chloride
20.0 mMHEPESN-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid
10.0 %CHAPS3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
10.0 mMD-desthiobiotinD-desthiobiotin
1.0 mMTCEPTris Carboxy Ethyl Phosphene
5.0 mMMgCl2magnesium chloride
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK I
DetailsThe sample was monodisperse

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Electron microscopy

MicroscopeTFS KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.8 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.42 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6qb8

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.2.1)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.2.1) / Number images used: 114711
FSC plot (resolution estimation)

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