[English] 日本語
Yorodumi
- EMDB-45886: TRiC-ADP-S2 state is a conformation when TRiC incubated in 1 mM ADP -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-45886
TitleTRiC-ADP-S2 state is a conformation when TRiC incubated in 1 mM ADP
Map dataTRiC-ADP-S2
Sample
  • Complex: TRiC at ADP state 2
    • Complex: T-complex protein 1 subunit gamma
      • Protein or peptide: T-complex protein 1 subunit gamma
    • Complex: the other TRiC subunits
      • 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 epsilon
      • Protein or peptide: T-complex protein 1 subunit eta
      • Protein or peptide: T-complex protein 1 subunit theta
      • Protein or peptide: T-complex protein 1 subunit zeta
      • Protein or peptide: T-complex protein 1 subunit delta
KeywordsComplex / Chaperonin / ADP / CHAPERONE
Function / homology
Function and homology information


Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / chaperonin-containing T-complex / : / Neutrophil degranulation / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding ...Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / chaperonin-containing T-complex / : / Neutrophil degranulation / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding / plasma membrane / 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. ...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 beta / T-complex protein 1 subunit gamma / T-complex protein 1 subunit delta / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit eta / T-complex protein 1 subunit theta
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.6 Å
AuthorsJin M / Cong Y
Funding support China, 2 items
OrganizationGrant numberCountry
National Basic Research Program of China (973 Program)2017YFA0503503 China
National Natural Science Foundation of China (NSFC)31670754, 31872714, and 31861143028 China
CitationJournal: QRB Discov / Year: 2025
Title: The conformational landscape of TRiC ring-opening and its underlying stepwise mechanism revealed by cryo-EM.
Authors: Mingliang Jin / Yunxiang Zang / Huping Wang / Yao Cong /
Abstract: The TRiC/CCT complex assists in the folding of approximately 10% of cytosolic proteins through an ATP-driven conformational cycle, playing a crucial role in maintaining protein homeostasis. Despite ...The TRiC/CCT complex assists in the folding of approximately 10% of cytosolic proteins through an ATP-driven conformational cycle, playing a crucial role in maintaining protein homeostasis. Despite our understanding of ATP-driven TRiC ring closing and substrate folding, the process and mechanisms underlying TRiC ring-opening and substrate release remain largely unexplored. In this study, by determining an ensemble of cryo-EM structures of yeast TRiC in the presence of ADP, including three intermediate transition states, we present a comprehensive picture of the TRiC ring-opening process. During this process, CCT3 detects the loss of γ-phosphate and initiates with the dynamics of its apical protrusion, and expands to the outward leaning of the consecutive CCT6/8/7/5 subunits. This is followed by significant movements of CCT2, CCT4, and especially CCT1 subunits, resulting in the opening of the TRiC rings. We also observed an unforeseen temporary separation between the two rings in the CCT2 side, coordinating the release of the originally locked CCT4 N-terminus, which potentially participates in the ring-opening process. Collectively, our study reveals a stepwise TRiC ring-opening mechanism, provides a comprehensive view of the TRiC conformational landscape, and sheds lights on its subunit specificity in sensing nucleotide status and substrate release. Our findings deepen our understanding of protein folding assisted by TRiC and may inspire new strategies for the diagnosis and treatment of related diseases.
History
DepositionJul 23, 2024-
Header (metadata) releaseJan 22, 2025-
Map releaseJan 22, 2025-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_45886.png

Downloads & links

-
Map

FileDownload / File: emd_45886.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTRiC-ADP-S2
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 256 pix.
= 337.408 Å		1.32 Å/pix.
x 256 pix.
= 337.408 Å		1.32 Å/pix.
x 256 pix.
= 337.408 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.318 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.5
Minimum - Maximum-1.0753927 - 2.3964624
Average (Standard dev.)0.021101676 (±0.13751763)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 337.408 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

+
Entire : TRiC at ADP state 2

EntireName: TRiC at ADP state 2
Components
  • Complex: TRiC at ADP state 2
    • Complex: T-complex protein 1 subunit gamma
      • Protein or peptide: T-complex protein 1 subunit gamma
    • Complex: the other TRiC subunits
      • 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 epsilon
      • Protein or peptide: T-complex protein 1 subunit eta
      • Protein or peptide: T-complex protein 1 subunit theta
      • Protein or peptide: T-complex protein 1 subunit zeta
      • Protein or peptide: T-complex protein 1 subunit delta

+
Supramolecule #1: TRiC at ADP state 2

SupramoleculeName: TRiC at ADP state 2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

+
Supramolecule #2: T-complex protein 1 subunit gamma

SupramoleculeName: T-complex protein 1 subunit gamma / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C

+
Supramolecule #3: the other TRiC subunits

SupramoleculeName: the other TRiC subunits / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#3, #5-#8
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C

+
Macromolecule #1: T-complex protein 1 subunit alpha

MacromoleculeName: T-complex protein 1 subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 60.557566 KDa
SequenceString: MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQ QDREIGDGTT SVVIIASELL KRANELVKNK IHPTTIITGF RVALREAIRF INEVLSTSVD TLGKETLINI A KTSMSSKI ...String:
MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQ QDREIGDGTT SVVIIASELL KRANELVKNK IHPTTIITGF RVALREAIRF INEVLSTSVD TLGKETLINI A KTSMSSKI IGADSDFFSN MVVDALLAVK TQNSKGEIKY PVKAVNVLKA HGKSATESLL VPGYALNCTV ASQAMPKRIA GG NVKIACL DLNLQKARMA MGVQINIDDP EQLEQIRKRE AGIVLERVKK IIDAGAQVVL TTKGIDDLCL KEFVEAKIMG VRR CKKEDL RRIARATGAT LVSSMSNLEG EETFESSYLG LCDEVVQAKF SDDECILIKG TSKHSSSSII LRGANDYSLD EMER SLHDS LSVVKRTLES GNVVPGGGCV EAALNIYLDN FATTVGSREQ LAIAEFAAAL LIIPKTLAVN AAKDSSELVA KLRSY HAAS QMAKPEDVKR RSYRNYGLDL IRGKIVDEIH AGVLEPTISK VKSLKSALEA CVAILRIDTM ITVDPEPPKE DPHDH

UniProtKB: T-complex protein 1 subunit alpha

+
Macromolecule #2: T-complex protein 1 subunit beta

MacromoleculeName: T-complex protein 1 subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 57.276254 KDa
SequenceString: MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG ATILKSIPLD NPAAKVLVNI SKVQDDEVG DGTTSVTVLS AELLREAEKL IDQSKIHPQT IIEGYRLASA AALDALTKAA VDNSHDKTMF REDLIHIAKT T LSSKILSQ ...String:
MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG ATILKSIPLD NPAAKVLVNI SKVQDDEVG DGTTSVTVLS AELLREAEKL IDQSKIHPQT IIEGYRLASA AALDALTKAA VDNSHDKTMF REDLIHIAKT T LSSKILSQ DKDHFAELAT NAILRLKGST NLEHIQIIKI LGGKLSDSFL DEGFILAKKF GNNQPKRIEN AKILIANTTL DT DKVKIFG TKFKVDSTAK LAQLEKAERE KMKNKIAKIS KFGINTFINR QLIYDYPEQL FTDLGINSIE HADFEGVERL ALV TGGEVV STFDEPSKCK LGECDVIEEI MLGEQPFLKF SGCKAGEACT IVLRGATDQT LDEAERSLHD ALSVLSQTTK ETRT VLGGG CAEMVMSKAV DTEAQNIDGK KSLAVEAFAR ALRQLPTILA DNAGFDSSEL VSKLRSSIYN GISTSGLDLN NGTIA DMRQ LGIVESYKLK RAVVSSASEA AEVLLRVDNI IRARPRTANR QHM

UniProtKB: T-complex protein 1 subunit beta

+
Macromolecule #3: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 61.995004 KDa
SequenceString: MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI IKTSLGPRGL DKILISPDGE ITITNDGAT ILSQMELDNE IAKLLVQLSK SQDDEIGDGT TGVVVLASAL LDQALELIQK GIHPIKIANG FDEAAKLAIS K LEETCDDI ...String:
MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI IKTSLGPRGL DKILISPDGE ITITNDGAT ILSQMELDNE IAKLLVQLSK SQDDEIGDGT TGVVVLASAL LDQALELIQK GIHPIKIANG FDEAAKLAIS K LEETCDDI SASNDELFRD FLLRAAKTSL GSKIVSKDHD RFAEMAVEAV INVMDKDRKD VDFDLIKMQG RVGGSISDSK LI NGVILDK DFSHPQMPKC VLPKEGSDGV KLAILTCPFE PPKPKTKHKL DISSVEEYQK LQTYEQDKFK EMIDDVKKAG ADV VICQWG FDDEANHLLL QNDLPAVRWV GGQELEHIAI STNGRIVPRF QDLSKDKLGT CSRIYEQEFG TTKDRMLIIE QSKE TKTVT CFVRGSNKMI VDEAERALHD SLCVVRNLVK DSRVVYGGGA AEVTMSLAVS EEADKQRGID QYAFRGFAQA LDTIP MTLA ENSGLDPIGT LSTLKSKQLK EKISNIGVDC LGYGSNDMKE LFVVDPFIGK KQQILLATQL CRMILKIDNV IISGKD EY

UniProtKB: T-complex protein 1 subunit epsilon

+
Macromolecule #4: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 65.423387 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND GHAILREIDV AHPAAKSMLE LSRTQDEEV GDGTTTVIIL AGEILAQCAP YLIEKNIHPV IIIQALKKAL TDALEVIKQV SKPVDVENDA AMKKLIQASI G TKYVIHWS ...String:
MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND GHAILREIDV AHPAAKSMLE LSRTQDEEV GDGTTTVIIL AGEILAQCAP YLIEKNIHPV IIIQALKKAL TDALEVIKQV SKPVDVENDA AMKKLIQASI G TKYVIHWS EKMCELALDA VKTVRKDLGQ TVEGEPNFEI DIKRYVRVEK IPGGDVLDSR VLKGVLLNKD VVHPKMSRHI EN PRVVLLD CPLEYKKGES QTNIEIEKEE DWNRILQIEE EQVQLMCEQI LAVRPTLVIT EKGVSDLAQH YLLKGGCSVL RRV KKSDNN RIARVTGATI VNRVEDLKES DVGTNCGLFK VEMIGDEYFS FLDNCKEPLE GSGSGWSHPQ FEKGSGKRRW KKNF IAVSA ANRFKKISSS GALGSGHHHH HHHHGSGLQK ACTIMLRGGS KDILNEIDRN LQDAMAVARN VMLSPSLSPG GGATE MAVS VKLAEKAKQL EGIQQWPYQA VADAMECIPR TLIQNAGGDP IRLLSQLRAK HAQGNFTTGI DGDKGKIVDM VSYGIW EPE VIKQQSVKTA IESACLLLRV DDIVSGVRKQ E

UniProtKB: T-complex protein 1 subunit gamma

+
Macromolecule #5: T-complex protein 1 subunit eta

MacromoleculeName: T-complex protein 1 subunit eta / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 59.802438 KDa
SequenceString: MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT TISNDGATIL KLLDVVHPAA KTLVDISRA QDAEVGDGTT SVTILAGELM KEAKPFLEEG ISSHLIMKGY RKAVSLAVEK INELAVDITS EKSSGRELLE R CARTAMSS ...String:
MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT TISNDGATIL KLLDVVHPAA KTLVDISRA QDAEVGDGTT SVTILAGELM KEAKPFLEEG ISSHLIMKGY RKAVSLAVEK INELAVDITS EKSSGRELLE R CARTAMSS KLIHNNADFF VKMCVDAVLS LDRNDLDDKL IGIKKIPGGA MEESLFINGV AFKKTFSYAG FEQQPKKFNN PK ILSLNVE LELKAEKDNA EVRVEHVEDY QAIVDAEWQL IFEKLRQVEE TGANIVLSKL PIGDLATQFF ADRNIFCAGR VSA DDMNRV IQAVGGSIQS TTSDIKPEHL GTCALFEEMQ IGSERYNLFQ GCPQAKTCTL LLRGGAEQVI AEVERSLHDA IMIV KRALQ NKLIVAGGGA TEMEVSKCLR DYSKTIAGKQ QMIINAFAKA LEVIPRQLCE NAGFDAIEIL NKLRLAHSKG EKWYG VVFE TENIGDNFAK FVWEPALVKI NALNSATEAT NLILSVDETI TNKGSESANA GMMPPQGAGR GRGMPM

UniProtKB: T-complex protein 1 subunit eta

+
Macromolecule #6: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 61.735102 KDa
SequenceString: MSLRLPQNPN AGLFKQGYNS YSNADGQIIK SIAAIRELHQ MCLTSMGPCG RNKIIVNHLG KIIITNDAAT MLRELDIVHP AVKVLVMAT EQQKIDMGDG TNLVMILAGE LLNVSEKLIS MGLSAVEIIQ GYNMARKFTL KELDEMVVGE ITDKNDKNEL L KMIKPVIS ...String:
MSLRLPQNPN AGLFKQGYNS YSNADGQIIK SIAAIRELHQ MCLTSMGPCG RNKIIVNHLG KIIITNDAAT MLRELDIVHP AVKVLVMAT EQQKIDMGDG TNLVMILAGE LLNVSEKLIS MGLSAVEIIQ GYNMARKFTL KELDEMVVGE ITDKNDKNEL L KMIKPVIS SKKYGSEDIL SELVSEAVSH VLPVAQQAGE IPYFNVDSIR VVKIMGGSLS NSTVIKGMVF NREPEGHVKS LS EDKKHKV AVFTCPLDIA NTETKGTVLL HNAQEMLDFS KGEEKQIDAM MKEIADMGVE CIVAGAGVGE LALHYLNRYG ILV LKVPSK FELRRLCRVC GATPLPRLGA PTPEELGLVE TVKTMEIGGD RVTVFKQEQG EISRTSTIIL RGATQNNLDD IERA IDDGV AAVKGLMKPS GGKLLPGAGA TEIELISRIT KYGERTPGLL QLAIKQFAVA FEVVPRTLAE TAGLDVNEVL PNLYA AHNV TEPGAVKTDH LYKGVDIDGE SDEGVKDIRE ENIYDMLATK KFAINVATEA ATTVLSIDQI IMAKKAGGPR APQGPR PGN WDQED

UniProtKB: T-complex protein 1 subunit theta

+
Macromolecule #7: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 59.997559 KDa
SequenceString: MSLQLLNPKA ESLRRDAALK VNVTSAEGLQ SVLETNLGPK GTLKMLVDGA GNIKLTKDGK VLLTEMQIQS PTAVLIARAA AAQDEITGD GTTTVVCLVG ELLRQAHRFI QEGVHPRIIT DGFEIARKES MKFLDEFKIS KTNLSNDREF LLQVARSSLL T KVDADLTE ...String:
MSLQLLNPKA ESLRRDAALK VNVTSAEGLQ SVLETNLGPK GTLKMLVDGA GNIKLTKDGK VLLTEMQIQS PTAVLIARAA AAQDEITGD GTTTVVCLVG ELLRQAHRFI QEGVHPRIIT DGFEIARKES MKFLDEFKIS KTNLSNDREF LLQVARSSLL T KVDADLTE VLTPIVTDAV LSVYDAQADN LDLHMVEIMQ MQHLSPKDTT FIKGLVLDHG GRHPDMPTRV KNAYVLILNV SL EYEKTEV NSGFFYSSAD QRDKLAASER KFVDAKLKKI IDLKNEVCGM DPDKGFVIIN QKGIDPMSLD VFAKHNILAL RRA KRRNME RLQLVTGGEA QNSVEDLSPQ ILGFSGLVYQ ETIGEEKFTY VTENTDPKSC TILIKGSTHY ALAQTKDAVR DGLR AVANV LKDKNIIPGA GAFYIALSRY LRSANMNKLG AKGKTKTGIE AFAEALLVIP KTLVKNSGFD PLDVLAMVED ELDDA QDSD ETRYVGVDLN IGDSCDPTIE GIWDSYRVLR NAITGATGIA SNLLLCDELL RAGRSTLKET PQ

UniProtKB: T-complex protein 1 subunit zeta

+
Macromolecule #8: T-complex protein 1 subunit delta

MacromoleculeName: T-complex protein 1 subunit delta / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: S288C
Molecular weightTheoretical: 57.68241 KDa
SequenceString: MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT SRGEIIISND GHTILKQMAI LHPVARMLVE VSAAQDSEA GDGTTSVVIL TGALLGAAER LLNKGIHPTI IADSFQSAAK RSVDILLEMC HKVSLSDREQ LVRAASTSLS S KIVSQYSS ...String:
MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT SRGEIIISND GHTILKQMAI LHPVARMLVE VSAAQDSEA GDGTTSVVIL TGALLGAAER LLNKGIHPTI IADSFQSAAK RSVDILLEMC HKVSLSDREQ LVRAASTSLS S KIVSQYSS FLAPLAVDSV LKISDENSKN VDLNDIRLVK KVGGTIDDTE MIDGVVLTQT AIKSAGGPTR KEKAKIGLIQ FQ ISPPKPD TENNIIVNDY RQMDKILKEE RAYLLNICKK IKKAKCNVLL IQKSILRDAV NDLALHFLSK LNIMVVKDIE REE IEFLSK GLGCKPIADI ELFTEDRLGS ADLVEEIDSD GSKIVRVTGI RNNNARPTVS VVIRGANNMI IDETERSLHD ALCV IRCLV KERGLIAGGG APEIEISRRL SKEARSMEGV QAFIWQEFAS ALEVIPTTLA ENAGLNSIKV VTELRSKHEN GELND GISV RRSGTTNTYE EHILQPVLVS TSAITLASEC VKSILRIDDI AFSR

UniProtKB: T-complex protein 1 subunit delta

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 38.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: NONE
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45923
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more