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- EMDB-40488: CCT G beta 5 complex closed state 5 -

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Open data


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Basic information

Entry
Database: EMDB / ID: EMD-40488
TitleCCT G beta 5 complex closed state 5
Map data
Sample
  • Complex: CCT-Gb5-PhLP1 in closed state 5
    • Protein or peptide: x 10 types
  • Ligand: x 4 types
KeywordsCCT / Gb5 / complex / open / CHAPERONE
Function / homology
Function and homology information


heterotrimeric G-protein complex assembly / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / zona pellucida receptor complex / scaRNA localization to Cajal body / positive regulation of protein localization to Cajal body / tubulin complex assembly ...heterotrimeric G-protein complex assembly / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / 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 / cell projection organization / binding of sperm to zona pellucida / regulation of G protein-coupled receptor signaling pathway / Prefoldin mediated transfer of substrate to CCT/TriC / positive regulation of smoothened signaling pathway / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / dopamine receptor signaling pathway / 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 / visual perception / GTPase activator activity / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / response to virus / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / mRNA 5'-UTR binding / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / cilium / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / positive regulation of GTPase activity / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / G-protein beta-subunit binding / heterotrimeric G-protein complex / Inactivation, recovery and regulation of the phototransduction cascade / G alpha (12/13) signalling events / azurophil granule lumen / melanosome / unfolded protein binding / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / protein folding / presynapse / cell body / Ca2+ pathway / G alpha (i) signalling events / protein-folding chaperone binding / G alpha (s) signalling events / G alpha (q) signalling events / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / Extra-nuclear estrogen signaling / protein stabilization / cytoskeleton / cadherin binding / G protein-coupled receptor signaling pathway / GTPase activity / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / Golgi apparatus / signal transduction / ATP hydrolysis activity / RNA binding
Similarity search - Function
Phosducin / Phosducin, N-terminal domain superfamily / Phosducin, thioredoxin-like domain / Phosducin / 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 ...Phosducin / Phosducin, N-terminal domain superfamily / Phosducin, thioredoxin-like domain / Phosducin / 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 / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / Thioredoxin-like superfamily / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Guanine nucleotide-binding protein subunit beta-5 / 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 / Phosducin-like protein / T-complex protein 1 subunit eta
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 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 14, 2023-
Header (metadata) releaseOct 25, 2023-
Map releaseOct 25, 2023-
UpdateNov 15, 2023-
Current statusNov 15, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40488.png

Downloads & links

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Map

FileDownload / File: emd_40488.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: 0.171
Minimum - Maximum-0.32695094 - 1.033568
Average (Standard dev.)0.00423469 (±0.046786413)
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: #2

Fileemd_40488_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_40488_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 closed state 5

EntireName: CCT-Gb5-PhLP1 in closed state 5
Components
  • Complex: CCT-Gb5-PhLP1 in closed state 5
    • Protein or peptide: Guanine nucleotide-binding protein subunit beta-5
    • Protein or peptide: T-complex protein 1 subunit alpha
    • 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
    • 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 zeta
    • Protein or peptide: Phosducin-like protein
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ALUMINUM FLUORIDEAluminium fluoride
  • Ligand: water

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Supramolecule #1: CCT-Gb5-PhLP1 in closed state 5

SupramoleculeName: CCT-Gb5-PhLP1 in closed state 5 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney / Tissue: Kidney

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Macromolecule #1: Guanine nucleotide-binding protein subunit beta-5

MacromoleculeName: Guanine nucleotide-binding protein subunit beta-5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 43.619297 KDa
SequenceString: MCDQTFLVNV FGSCDKCFKQ RALRPVFKKS QQLSYCSTCA EIMATEGLHE NETLASLKSE AESLKGKLEE ERAKLHDVEL HQVAERVEA LGQFVMKTRR TLKGHGNKVL CMDWCKDKRR IVSSSQDGKV IVWDSFTTNK EHAVTMPCTW VMACAYAPSG C AIACGGLD ...String:
MCDQTFLVNV FGSCDKCFKQ RALRPVFKKS QQLSYCSTCA EIMATEGLHE NETLASLKSE AESLKGKLEE ERAKLHDVEL HQVAERVEA LGQFVMKTRR TLKGHGNKVL CMDWCKDKRR IVSSSQDGKV IVWDSFTTNK EHAVTMPCTW VMACAYAPSG C AIACGGLD NKCSVYPLTF DKNENMAAKK KSVAMHTNYL SACSFTNSDM QILTASGDGT CALWDVESGQ LLQSFHGHGA DV LCLDLAP SETGNTFVSG GCDKKAMVWD MRSGQCVQAF ETHESDINSV RYYPSGDAFA SGSDDATCRL YDLRADREVA IYS KESIIF GASSVDFSLS GRLLFAGYND YTINVWDVLK GSRVSILFGH ENRVSTLRVS PDGTAFCSGS WDHTLRVWA

UniProtKB: Guanine nucleotide-binding protein subunit beta-5

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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 beta

MacromoleculeName: T-complex protein 1 subunit beta / type: protein_or_peptide / ID: 3 / 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 #4: T-complex protein 1 subunit delta

MacromoleculeName: T-complex protein 1 subunit delta / type: protein_or_peptide / ID: 4 / 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 #5: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 5 / 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 #6: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / 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 #7: T-complex protein 1 subunit eta, N-terminally processed

MacromoleculeName: T-complex protein 1 subunit eta, N-terminally processed
type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 57.939809 KDa
SequenceString: MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI ...String:
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI SQQKAFFAKM VVDAVMMLDD LLQLKMIGIK KVQGGALEDS QLVAGVAFKK TFSYAGFEMQ PKKYHNPKIA LL NVELELK AEKDNAEIRV HTVEDYQAIV DAEWNILYDK LEKIHHSGAK VVLSKLPIGD VATQYFADRD MFCAGRVPEE DLK RTMMAC GGSIQTSVNA LSADVLGRCQ VFEETQIGGE RYNFFTGCPK AKTCTFILRG GAEQFMEETE RSLHDAIMIV RRAI KNDSV VAGGGAIEME LSKYLRDYSR TIPGKQQLLI GAYAKALEII PRQLCDNAGF DATNILNKLR ARHAQGGTWY GVDIN NEDI ADNFEAFVWE PAMVRINALT AASEAACLIV SVDETIKNPR STVD

UniProtKB: T-complex protein 1 subunit eta

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Macromolecule #8: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 58.427164 KDa
SequenceString: ALHVPKAPGF AQMLKEGAKH FSGLEEAVYR NIQACKELAQ TTRTAYGPNG MNKMVINHLE KLFVTNDAAT ILRELEVQHP AAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV S SLLRTSIM ...String:
ALHVPKAPGF AQMLKEGAKH FSGLEEAVYR NIQACKELAQ TTRTAYGPNG MNKMVINHLE KLFVTNDAAT ILRELEVQHP AAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV S SLLRTSIM SKQYGNEVFL AKLIAQACVS IFPDSGHFNV DNIRVCKILG SGISSSSVLH GMVFKKETEG DVTSVKDAKI AV YSCPFDG MITETKGTVL IKTAEELMNF SKGEENLMDA QVKAIADTGA NVVVTGGKVA DMALHYANKY NIMLVRLNSK WDL RRLCKT VGATALPRLT PPVLEEMGHC DSVYLSEVGD TQVVVFKHEK EDGAISTIVL RGSTDNLMDD IERAVDDGVN TFKV LTRDK RLVPGGGATE IELAKQITSY GETCPGLEQY AIKKFAEAFE AIPRALAENS GVKANEVISK LYAVHQEGNK NVGLD IEAE VPAVKDMLEA GILDTYLGKY WAIKLATNAA VTVLRVDQII MAKPAGGPKP PSGK

UniProtKB: T-complex protein 1 subunit theta

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Macromolecule #9: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 57.719613 KDa
SequenceString: MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL ...String:
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL TEAVVDSILA IKKQDEPIDL FMIEIMEMKH KSETDTSLIR GLVLDHGARH PDMKKRVEDA YILTCNVSLE YE KTEVNSG FFYKSAEERE KLVKAERKFI EDRVKKIIEL KRKVCGDSDK GFVVINQKGI DPFSLDALSK EGIVALRRAK RRN MERLTL ACGGVALNSF DDLSPDCLGH AGLVYEYTLG EEKFTFIEKC NNPRSVTLLI KGPNKHTLTQ IKDAVRDGLR AVKN AIDDG CVVPGAGAVE VAMAEALIKH KPSVKGRAQL GVQAFADALL IIPKVLAQNS GFDLQETLVK IQAEHSESGQ LVGVD LNTG EPMVAAEVGV WDNYCVKKQL LHSCTVIATN ILLVDEIMRA GMS

UniProtKB: T-complex protein 1 subunit zeta

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Macromolecule #10: Phosducin-like protein

MacromoleculeName: Phosducin-like protein / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney
Molecular weightTheoretical: 34.322527 KDa
SequenceString: MTTLDDKLLG EKLQYYYSSS EDEDSDHEDK DRGRCAPASS SVPAEAELAG EGISVNTGPK GVINDWRRFK QLETEQREEQ CREMERLIK KLSMTCRSHL DEEEEQQKQK DLQEKISGKM TLKEFAIMNE DQDDEEFLQQ YRKQRMEEMR QQLHKGPQFK Q VFEISSGE ...String:
MTTLDDKLLG EKLQYYYSSS EDEDSDHEDK DRGRCAPASS SVPAEAELAG EGISVNTGPK GVINDWRRFK QLETEQREEQ CREMERLIK KLSMTCRSHL DEEEEQQKQK DLQEKISGKM TLKEFAIMNE DQDDEEFLQQ YRKQRMEEMR QQLHKGPQFK Q VFEISSGE GFLDMIDKEQ KSIVIMVHIY EDGIPGTEAM NGCMICLAAE YPAVKFCKVK SSVIGASSQF TRNALPALLI YK GGELIGN FVRVTDQLGD DFFAVDLEAF LQEFGLLPEK EVLVLTSVRN SATCHSEDSD LEID

UniProtKB: Phosducin-like protein

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Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / 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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Macromolecule #12: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 12 / Number of copies: 16 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #13: ALUMINUM FLUORIDE

MacromoleculeName: ALUMINUM FLUORIDE / type: ligand / ID: 13 / Number of copies: 16 / Formula: AF3
Molecular weightTheoretical: 83.977 Da
Chemical component information

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

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Macromolecule #14: water

MacromoleculeName: water / type: ligand / ID: 14 / Number of copies: 19 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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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: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.2.1) / Number images used: 44618
FSC plot (resolution estimation)

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